Updated on 2022/05/23

写真a

 
NOZUMI Motohiro
 
Organization
Academic Assembly Institute of Medicine and Dentistry IGAKU KEIRETU Lecturer
Faculty of Medicine School of Medicine Lecturer
Graduate School of Medical and Dental Sciences Molecular and Cellular Medicine Lecturer
Title
Lecturer
▶ display Profile on researchmap
External link

Degree

  • 博士(情報工学) ( 2003.3   九州工業大学 )

Research Interests

  • Endocytosis

  • Actin

  • Axon guidance

  • 包括脳ネットワーク

  • Cytoskeleton

  • Organelles

  • 3D-STED

  • 3D-SIM

  • Super-resolution microscopy

  • Membrane trafficking

  • Cell motility

  • Growth cone

Research Areas

  • Life Science / Cell biology

  • Life Science / Neuroscience-general

Research History (researchmap)

  • Universite de Bordeaux   Institute for Interdisciplinary Neuroscience   Visiting researcher

    2021.1 - 2021.6

      More details

    Country:France

    researchmap

  • Universite de Bordeaux   Institute for Interdisciplinary Neuroscience   Visiting researcher

    2019.7 - 2019.12

      More details

    Country:France

    researchmap

  • Niigata University   Department of Neurochemistry   Lecturer

    2011.6

      More details

  • Niigata University   Department of Neurochemistry   Assistant Professor

    2008.4 - 2011.5

      More details

  • Niigata University   Department of Neurochemistry   Researcher

    2005.4 - 2008.3

      More details

  • National Institute of Genetics   Division of Brain Function   Researcher

    2003.4 - 2005.3

      More details

  • 九州工業大学大学院 情報工学研究科   博士(情報工学) 取得

    2003.3

      More details

▶ display all

Research History

  • Niigata University   Faculty of Medicine School of Medicine   Lecturer

    2011.6

  • Niigata University   Graduate School of Medical and Dental Sciences Molecular and Cellular Medicine   Lecturer

    2011.6

  • Niigata University   Graduate School of Medical and Dental Sciences Molecular and Cellular Medicine   Assistant Professor

    2007.4 - 2011.5

Professional Memberships

 

Papers

  • Phosphorylation of GAP-43 T172 is a molecular marker of growing axons in a wide range of mammals including primates. Reviewed International journal

    Masayasu Okada, Yosuke Kawagoe, Yuta Sato, Motohiro Nozumi, Yuya Ishikawa, Atsushi Tamada, Hiroyuki Yamazaki, Yuko Sekino, Yonehiro Kanemura, Yohei Shinmyo, Hiroshi Kawasaki, Naoko Kaneko, Kazunobu Sawamoto, Yukihiko Fujii, Michihiro Igarashi

    Molecular brain   14 ( 1 )   66 - 66   2021.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    GAP-43 is a vertebrate neuron-specific protein and that is strongly related to axon growth and regeneration; thus, this protein has been utilized as a classical molecular marker of these events and growth cones. Although GAP-43 was biochemically characterized more than a quarter century ago, how this protein is related to these events is still not clear. Recently, we identified many phosphorylation sites in the growth cone membrane proteins of rodent brains. Two phosphorylation sites of GAP-43, S96 and T172, were found within the top 10 hit sites among all proteins. S96 has already been characterized (Kawasaki et al., 2018), and here, phosphorylation of T172 was characterized. In vitro (cultured neurons) and in vivo, an antibody specific to phosphorylated T172 (pT172 antibody) specifically recognized cultured growth cones and growing axons in developing mouse neurons, respectively. Immunoblotting showed that pT172 antigens were more rapidly downregulated throughout development than those of pS96 antibody. From the primary structure, this phosphorylation site was predicted to be conserved in a wide range of animals including primates. In the developing marmoset brainstem and in differentiated neurons derived from human induced pluripotent stem cells, immunoreactivity with pT172 antibody revealed patterns similar to those in mice. pT172 antibody also labeled regenerating axons following sciatic nerve injury. Taken together, the T172 residue is widely conserved in a wide range of mammals including primates, and pT172 is a new candidate molecular marker for growing axons.

    DOI: 10.1186/s13041-021-00755-0

    PubMed

    researchmap

  • Coactosin Promotes F-Actin Protrusion in Growth Cones Under Cofilin-Related Signaling Pathway. Reviewed International journal

    Xubin Hou, Motohiro Nozumi, Harukazu Nakamura, Michihiro Igarashi, Sayaka Sugiyama

    Frontiers in cell and developmental biology   9   660349 - 660349   2021

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    During brain development, axon outgrowth and its subsequent pathfinding are reliant on a highly motile growth cone located at the tip of the axon. Actin polymerization that is regulated by actin-depolymerizing factors homology (ADF-H) domain-containing family drives the formation of lamellipodia and filopodia at the leading edge of growth cones for axon guidance. However, the precise localization and function of ADF-H domain-containing proteins involved in axon extension and retraction remain unclear. We have previously shown that transcripts and proteins of coactosin-like protein 1 (COTL1), an ADF-H domain-containing protein, are observed in neurites and axons in chick embryos. Coactosin overexpression analysis revealed that this protein was localized to axonal growth cones and involved in axon extension in the midbrain. We further examined the specific distribution of coactosin and cofilin within the growth cone using superresolution microscopy, structured illumination microscopy, which overcomes the optical diffraction limitation and is suitable to the analysis of cellular dynamic movements. We found that coactosin was tightly associated with F-actin bundles at the growth cones and that coactosin overexpression promoted the expansion of lamellipodia and extension of growth cones. Coactosin knockdown in oculomotor neurons resulted in an increase in the levels of the inactive, phosphorylated form of cofilin and dysregulation of actin polymerization and axonal elongation, which suggests that coactosin promoted axonal growth in a cofilin-dependent manner. Indeed, the application of a dominant-negative form of LIMK1, a downstream effector of GTPases, reversed the effect of coactosin knockdown on axonal growth by enhancing cofilin activity. Combined, our results indicate that coactosin functions promote the assembly of protrusive actin filament arrays at the leading edge for growth cone motility.

    DOI: 10.3389/fcell.2021.660349

    PubMed

    researchmap

  • Isoform-dependent subcellular localization of LMTK1A and LMTK1B and their roles in axon outgrowth and spine formation. Reviewed International journal

    Ran Wei, Arika Sugiyama, Yuta Sato, Motohiro Nozumi, Hironori Nishino, Miyuki Takahashi, Taro Saito, Kanae Ando, Mitsunori Fukuda, Mineko Tomomura, Michihiro Igarashi, Shin-Ichi Hisanaga

    Journal of biochemistry   168 ( 1 )   23 - 32   2020.7

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Lemur kinase 1 (LMTK1) is a membrane-bound Ser/Thr kinase that is expressed in neurons. There are two splicing variants of LMTK1 with different membrane binding modes, viz., cytosolic LMTK1A that binds to membranes through palmitoylation at the N-terminal cysteines and LMTK1B, an integral membrane protein with transmembrane sequences. We recently reported that LMTK1A regulates axon outgrowth and spine formation in neurons. However, data about LMTK1B are scarce. We analysed the expression and cellular localization of LMTK1B along with its role in axon and spine formation. We found that both LMTK1B and LMTK1A were expressed equally in the cerebral cortex and cerebellum of the mouse brain. Similar to LMTK1A, the wild type of LMTK1B was localized to Rab11-positive pericentrosomal compartment. The kinase negative (kn) mutant of LMTK1B was found to be associated with an increase in the tubular form of endoplasmic reticulum (ER), which was not the case with LMTK1A kn. Furthermore, unlike LMTK1A kn, LMTK1B kn did not stimulate the axon outgrowth and spine formation. These results suggest that while LMTK1A and LMTK1B share a common function in recycling endosomal trafficking at the pericentrosomal compartment, LMTK1B has an additional unique function in vesicle transport in the ER region.

    DOI: 10.1093/jb/mvaa019

    PubMed

    researchmap

  • Microtubule elongation along actin filaments induced by microtubule-associated protein 4 contributes to the formation of cellular protrusions. Reviewed International journal

    Chihiro Doki, Kohei Nishida, Shoma Saito, Miyuki Shiga, Hikari Ogara, Ayumu Kuramoto, Masahiro Kuragano, Motohiro Nozumi, Michihiro Igarashi, Hiroyuki Nakagawa, Susumu Kotani, Kiyotaka Tokuraku

    Journal of biochemistry   168 ( 3 )   295 - 303   2020.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Actin-microtubule crosstalk is implicated in the formation of cellular protrusions, but the mechanism remains unclear. In this study, we examined the regulation of cell protrusion involving a ubiquitously expressed microtubule-associated protein (MAP) 4, and its superfamily proteins, neuronal MAP2 and tau. Fluorescence microscopy revealed that these MAPs bound to F-actin and microtubules simultaneously, and formed F-actin/microtubule hybrid bundles. The hybrid bundle-forming activity was in the order of MAP2 > MAP4 ≫ tau. Interestingly, the microtubule assembly-promoting activity of MAP4 and MAP2, but not of tau, was upregulated by their interaction with F-actin. When MAP4 was overexpressed in NG108-15 cells, the number of cell processes and maximum process length of each cell increased significantly by 28% and 30%, respectively. Super-resolution microscopy revealed that 95% of microtubules in cell processes colocalized with F-actin, and MAP4 was always found in their vicinity. These results suggest that microtubule elongation along F-actin induced by MAP4 contributes to the formation of cellular protrusions. Since MAP4, MAP2, and tau had different crosstalk activity between F-actin and microtubules, it is likely that the functional differentiation of these MAPs is a driving force for neural evolution, causing significant changes in cell morphology.

    DOI: 10.1093/jb/mvaa046

    PubMed

    researchmap

  • Neuronal Signaling Involved in Neuronal Polarization and Growth: Lipid Rafts and Phosphorylation. Reviewed International journal

    Michihiro Igarashi, Atsuko Honda, Asami Kawasaki, Motohiro Nozumi

    Frontiers in molecular neuroscience   13   150 - 150   2020

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    Neuronal polarization and growth are developmental processes that occur during neuronal cell differentiation. The molecular signaling mechanisms involved in these events in in vivo mammalian brain remain unclear. Also, cellular events of the neuronal polarization process within a given neuron are thought to be constituted of many independent intracellular signal transduction pathways (the "tug-of-war" model). However, in vivo results suggest that such pathways should be cooperative with one another among a given group of neurons in a region of the brain. Lipid rafts, specific membrane domains with low fluidity, are candidates for the hotspots of such intracellular signaling. Among the signals reported to be involved in polarization, a number are thought to be present or translocated to the lipid rafts in response to extracellular signals. As part of our analysis, we discuss how such novel molecular mechanisms are combined for effective regulation of neuronal polarization and growth, focusing on the significance of the lipid rafts, including results based on recently introduced methods.

    DOI: 10.3389/fnmol.2020.00150

    PubMed

    researchmap

  • Vesicular movements in the growth cone. Reviewed

    Nozumi M, Igarashi M

    Neurochemistry international   119   71 - 76   2018.10

  • New observations in neuroscience using superresolution microscopy Reviewed

    Igarashi M, Nozumi M, Wu LG, Cella Zanacchi F, Katona I, Barna L, Xu P, Zhang M, Xue F, Boyden E

    The Journal of Neuroscience   38 ( 44 )   9459 - 9467   2018.10

  • Growth Cone Phosphoproteomics Reveals that GAP-43 Phosphorylated by JNK Is a Marker of Axon Growth and Regeneration. Reviewed International journal

    Asami Kawasaki, Masayasu Okada, Atsushi Tamada, Shujiro Okuda, Motohiro Nozumi, Yasuyuki Ito, Daiki Kobayashi, Tokiwa Yamasaki, Ryo Yokoyama, Takeshi Shibata, Hiroshi Nishina, Yutaka Yoshida, Yukihiko Fujii, Kosei Takeuchi, Michihiro Igarashi

    iScience   4   190 - 203   2018.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Elsevier {BV}  

    Neuronal growth cones are essential for nerve growth and regeneration, as well as for the formation and rearrangement of the neural network. To elucidate phosphorylation-dependent signaling pathways and establish useful molecular markers for axon growth and regeneration, we performed a phosphoproteomics study of mammalian growth cones, which identified >30,000 phosphopeptides of ∼1,200 proteins. The phosphorylation sites were highly proline directed and primarily MAPK dependent, owing to the activation of JNK, suggesting that proteins that undergo proline-directed phosphorylation mediate nerve growth in the mammalian brain. Bioinformatics analysis revealed that phosphoproteins were enriched in microtubules and the cortical cytoskeleton. The most frequently phosphorylated site was S96 of GAP-43 (growth-associated protein 43-kDa), a vertebrate-specific protein involved in axon growth. This previously uncharacterized phosphorylation site was JNK dependent. S96 phosphorylation was specifically detected in growing and regenerating axons as the most frequent target of JNK signaling; thus it represents a promising new molecular marker for mammalian axonal growth and regeneration.

    DOI: 10.1016/j.isci.2018.05.019

    PubMed

    researchmap

  • Extracellular Signals Induce Glycoprotein M6a Clustering of Lipid Rafts and Associated Signaling Molecules Reviewed

    Atsuko Honda, Yasuyuki Ito, Kazuko Takahashi-Niki, Natsuki Matsushita, Motohiro Nozumi, Hidenori Tabata, Kosei Takeuchi, Michihiro Igarashi

    JOURNAL OF NEUROSCIENCE   37 ( 15 )   4046 - 4064   2017.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:SOC NEUROSCIENCE  

    Lipid raft domains, where sphingolipids and cholesterol are enriched, concentrate signaling molecules. Toexaminehowsignaling protein complexes are clustered in rafts, we focused on the functions of glycoprotein M6a (GPM6a), which is expressed at a high concentration in developing mouse neurons. Using imaging of lipid rafts, we found that GPM6a congregated in rafts in a GPM6a palmitoylation-dependent manner, thereby contributing to lipid raft clustering. In addition, we found that signaling proteins downstream of GPM6a, such as Rufy3, Rap2, and Tiam2/STEF, accumulated in lipid rafts in a GPM6a-dependent manner and were essential for laminin-dependent polarity during neurite formation in neuronal development. In utero RNAi targeting of GPM6a resulted in abnormally polarized neurons with multiple neurites. These results demonstrate that GPM6a induces the clustering of lipid rafts, which supports the raft aggregation of its associated downstream molecules for acceleration of neuronal polarity determination. Therefore, GPM6a acts as a signal transducer that responds to extracellular signals.

    DOI: 10.1523/JNEUROSCI.3319-16.2017

    Web of Science

    Scopus

    PubMed

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • Coordinated Movement of Vesicles and Actin Bundles during Nerve Growth Revealed by Superresolution Microscopy Reviewed

    Motohiro Nozumi, Fubito Nakatsu, Kaoru Katoh, Michihiro Igarashi

    CELL REPORTS   18 ( 9 )   2203 - 2216   2017.2

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:CELL PRESS  

    The growth cone is an essential structure for nerve growth. Although its membrane and cytoskeleton are likely to interact coordinately during nerve growth, the mechanisms are unknown due to their close proximity. Here, we used superresolution microscopy to simultaneously observe vesicles and F-actin in growth cones. We identified a novel vesicular generation mechanism that is independent of clathrin and dependent on endophilin-3-and dynamin-1 and that occurs proximal to the leading edge simultaneously with fascin-1-dependent F-actin bundling. In contrast to conventional clathrin-dependent endocytosis, which occurs distal from the leading edge at the basal surfaces of growth cones, this mechanism was distinctly observed at the apical surface using 3D imaging and was involved in mediating axon growth. Reduced endophilin or fascin inhibited this endocytic mechanism. These results suggest that, at the leading edge, vesicles are coordinately generated and transported with actin bundling during nerve growth.

    DOI: 10.1016/j.celrep.2017.02.008

    Web of Science

    Scopus

    PubMed

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • Expression and function of neuronal growth-associated proteins (nGAPs) in PC12 cells Reviewed

    Jia Lu, Motohiro Nozumi, Kosei Takeuchi, Haruki Abe, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   70 ( 1 )   85 - 90   2011.5

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ELSEVIER IRELAND LTD  

    The growth cone plays crucial roles in neural wiring, synapse formation, and axonal regeneration. Continuous rearrangement of cytoskeletal elements and targeting of transported vesicles to the plasma membrane are essential to growth cone motility; however, the proteins directly involved in these processes and their specific functions are not well established. We recently identified 17 proteins as functional marker proteins of the mammalian growth cone and as neuronal growth-associated proteins in rat cortical neurons (nGAPs; Nozumi et al., 2009). To determine whether these 17 proteins are growth cone markers in other neuronal cell types, we examined their expression and function in PC12D cells. We found that all 17 nGAPs were highly concentrated in the growth cones of PC12D cells, and that knockdown of all of them by RNAi reduced or inhibited neurite outgrowth, indicating that all of the 17 nGAPs may be general growth cone markers. Among them, eight proteins were shown to regulate the amount of F-actin in PC12D growth cones. Two of these nGAP that are cytoskeletal proteins. Cap1 and Sept2, increased the mean growth cone area and the mean neurite length by regulating the amount of F-actin; Sept2 also induced filopodial growth. Taken together, our data suggested that some of the nGAPs were generalized markers of the growth cone in multiple neuronal cell types and some of them, such as Cap1 and Sept2, regulated growth cone morphology through rearrangement of F-actin and thereby controlled neurite outgrowth. (C) 2011 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved.

    DOI: 10.1016/j.neures.2011.01.006

    Web of Science

    Scopus

    PubMed

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • A stochastic model of neuronal growth cone guidance regulated by multiple sensors Reviewed

    Taichiro Kobayashi, Kenshi Terajima, Motohiro Nozumi, Michihiro Igarashi, Kouhei Akazawa

    JOURNAL OF THEORETICAL BIOLOGY   266 ( 4 )   712 - 722   2010.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD  

    Neuronal growth cones migrate directionally under the control of axon guidance molecules, thereby forming synapses in the developing brain. The signal transduction system by which a growth cone detects surrounding guidance molecules, analyzes the detected signals, and then determines the overall behavior remains undetermined. In this study, we describe a novel stochastic model of this behavior that utilizes multiple sensors on filopodia to respond to guidance molecules. Overall growth cone behavior is determined by using only the concentration gradients of guidance molecules in the immediate vicinity of each sensor. The detected signal at each sensor, which is treated as a vector quantity, is sent to the growth cone center and then integrated to determine axonal growth in the next step by means of a simple vector operation. We compared the results of computer simulations of axonal growth with observations of actual axonal growth from co-culture experiments using olfactory bulb and septum. The probabilistic distributions of axonal growth generated by the computer simulation were consistent with those obtained from the culture experiments, indicating that our model accurately simulates growth cone behavior. We believe that this model will be useful for elucidating the as yet unknown mechanisms responsible for axonal growth in vivo. (c) 2010 Elsevier Ltd. All rights reserved.

    DOI: 10.1016/j.jtbi.2010.07.036

    Web of Science

    Scopus

    PubMed

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • Identification of functional marker proteins in the mammalian growth cone Reviewed

    Motohiro Nozumi, Tetsuya Togano, Kazuko Takahashi-Niki, Jia Lu, Atsuko Honda, Masato Taoka, Takashi Shinkawa, Hisashi Koga, Kosei Takeuchi, Toshiaki Isobe, Michihiro Igarashi

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   106 ( 40 )   17211 - 17216   2009.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATL ACAD SCIENCES  

    Identification of proteins in the mammalian growth cone has the potential to advance our understanding of this critical regulator of neuronal growth and formation of neural circuit; however, to date, only one growth cone marker protein, GAP-43, has been reported. Here, we successfully used a proteomic approach to identify 945 proteins present in developing rat forebrain growth cones, including highly abundant, membrane-associated and actin-associated proteins. Almost 100 of the proteins appear to be highly enriched in the growth cone, as determined by quantitative immunostaining, and for 17 proteins, the results of RNAi suggest a role in axon growth. Most of the proteins we identified have not previously been implicated in axon growth and thus their identification presents a significant step forward, providing marker proteins and candidate neuronal growth-associated proteins.

    DOI: 10.1073/pnas.0904092106

    Web of Science

    Scopus

    PubMed

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • A novel method for RNA interference in neurons using enhanced green fluorescent protein (EGFP)-transgenic rats Reviewed

    Jia Lu, Motohiro Nozumi, Hiroshi Fujii, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   61 ( 2 )   219 - 224   2008.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ELSEVIER IRELAND LTD  

    RNA interference (RNAi) is the simplest way of examining gene function by inhibiting expression. However, due to the low rate of introducing short interfering RNA (siRNA) into neurons, it is difficult to discriminate into which neurons that have been successfully introduced. Here, we used neurons from transgenic rats expressing enhanced green fluorescent protein (EGFP), and we simultaneously applied small interfering RNAs (siRNAs) against EGFP and a targeted gene to the EGFP-expressing neurons. EGFP fluorescence and immunoreactivity of the protein were then assessed by immunofluorescence microscopy. Quantitative analysis of the immunofluorescence confirmed that loss of EGFP closely correlates with loss of the target protein. These results indicate that this method can be used in a wider range of the neuroscientific research, especially in genome-wide studies. (c) 2008 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved.

    DOI: 10.1016/j.neures.2008.02.008

    Web of Science

    Scopus

    PubMed

    CiNii Article

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • IRSp53 is colocalised with WAVE2 at the tips of protruding lamellipodia and filopodia independently of Mena Reviewed

    H Nakagawa, H Miki, M Nozumi, T Takenawa, S Miyamoto, J Wehland, JV Small

    JOURNAL OF CELL SCIENCE   116 ( 12 )   2577 - 2583   2003.6

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:COMPANY OF BIOLOGISTS LTD  

    The insulin receptor tyrosine kinase substrate p53 (IRSp53) links Rac and WAVE2 and has been implicated in lamellipodia. protrusion. Recently, however, IRSp53 has been reported to bind to both Cdc42 and Mena to induce filopodia. To shed independent light on IRSp53 function we determined the localisations and dynamics of IRSp53 and WAVE2 in B16 melanoma cells. In cells spread well on a laminin substrate, IRSp53 was localised by antibody labelling at the tips of both lamellipodia and filopodia. The same localisation was observed in living cells with IRSp53 tagged with enhanced green florescence protein (EGFP-IRSp53), but only during protrusion. From the transfection of deletion mutants the N-terminal region of IRSp53, which binds active Rac, was shown to be responsible for its localisation. Although IRSp53 has been reported to regulate filopodia formation with Mena, EGFP-IRSp53,showed the same localisation in MVD7 Ena/VASP (vasodilator stimulated phosphoprotein) family deficient cells. WAVE2 tagged with DsRed1 colocalised with EGFP-IRSp53 at the tips of protruding lamellipodia and filopodia and, in double-transfected cells, the IRSp53 signal in filopodia decreased before that of WAVE2 during retraction. These results suggest an alternative modulatory role for IRSp53 in the extension of both filopodia and lamellipodia, through WAVE2.

    DOI: 10.1242/jcs.00462

    Web of Science

    Scopus

    PubMed

    CiNii Article

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

  • Differential localization of WAVE isoforms in filopodia and lamellipodia of the neuronal growth cone Reviewed

    M Nozumi, H Nakagawa, H Miki, T Takenawa, S Miyamoto

    JOURNAL OF CELL SCIENCE   116 ( 2 )   239 - 246   2003.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:COMPANY OF BIOLOGISTS LTD  

    The formation and extension of filopodia in response to an extracellular stimulus by guidance cues determine the path of growth cone advance. Actin-filament bundling and actin polymerization at the tips supply the driving force behind the formation and elongation. We tried to clarify how signals in response to extracellular cues are transformed to induce filopodial generation and extension. Observations on the formation process of filopodia at growth cones in the neuroblastoma cell line NG108 showed that WAVE (WASP (Wiskott-Aldrich syndrome protein)-family verprolin homologous protein) isoforms played crucial and distinct roles in this process. WAVE1 was continuously distributed along the leading edge only and was not found in the filopodia. WAVE2 and WAVE3 discretely localized at the initiation sites of microspikes on the leading edge and also concentrated at the tips of protruding filopodia. We further found that WAVE isoforms localized at the filopodial tips through SHD (SCAR homology domain), next to its leucine zipper-like motif. Furthermore, time-lapse observations of filopodial formation in living cells showed that WAVE2 and WAVE3 were continuously expressed at the tips of filopodia during elongation. These results indicate that WAVE2 or WAVE3 may guide the actin bundles into the filopodia and promote actin assembly at the tips.

    DOI: 10.1242/jcs.00233

    Web of Science

    Scopus

    PubMed

    CiNii Article

    J-GLOBAL

    researchmap

    Other Link: http://orcid.org/0000-0001-5972-2719

▶ display all

MISC

  • リン酸化プロテオミクスで同定された、神経成長関連分子群の責任キナーゼの解析

    河嵜 麻実, 小林 大記, 岡田 正康, 野住 素広, 武内 恒成, 五十嵐 道弘

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [4T17L - 12(3P0403)]   2015.12

     More details

    Language:Japanese   Publisher:(公社)日本生化学会  

    researchmap

  • Membrane retrieval coincides with the filopodia formation in the neuronal growth cone.

    M. Nozumi, M. Igarashi

    MOLECULAR BIOLOGY OF THE CELL   25   2014.12

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:AMER SOC CELL BIOLOGY  

    Web of Science

    researchmap

  • Functions of newly identified nerve growth-associated proteins in the growth cone

    Motohiro Nozumi, Jia Lu, Kosei Takeuchi, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   65   S97 - S97   2009

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER IRELAND LTD  

    DOI: 10.1016/j.neures.2009.09.415

    Web of Science

    researchmap

  • RNAi-mediated knockdown of FABP-7 inhibits neurite outgrowth in developing cortical neurons

    Jia Lu, Motohiro Nozumi, Haruki Abe, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   61   S233 - S233   2008

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER IRELAND LTD  

    Web of Science

    researchmap

  • Dynamics of actin-associated proteins detected by proteomics of growth cone

    Satoe Ebihara, Shirakawa Sayurni, Todaka Reiko, Nozumi Motohiro, Ozawa Mutsumi, Igarshi Michihiro, Katoh Kaoru

    NEUROSCIENCE RESEARCH   61   S89 - S89   2008

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER IRELAND LTD  

    Web of Science

    researchmap

  • 2P221 成長円錐のプロテオミクスで同定されたアクチン関連蛋白質は10タイプの動態を示す(細胞生物的課題(接着・運動・骨格・伝達・膜),口頭発表,第45回日本生物物理学会年会)

    海老原利枝, 白川彩弓, 戸高玲子, 野住素広, 小澤睦, 五十嵐道弘, 加藤薫

    生物物理   47 ( 1 )   2007.11

     More details

    Publisher:日本生物物理学会  

    CiNii Article

    researchmap

  • Imaging of f-actin and actin associate proteins in neuronal growth cones Reviewed

    Katoh Kaoru, Shirakawa Sayumi, Todaka Reiko, Miyoshi Hiromi, Ozawa Mutsumi, Nozumi Motohiro, Igarashi Michihiro

    Journal of Pharmacological Sciences   103   47P   2007

  • Systematic immunostaining and RNAi experiments for finding the novel molecular marker candidates of the growth cone

    Motohiro Nozumi, Kazuko Takahashi-Niki, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   58   S201 - S201   2007

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER IRELAND LTD  

    Web of Science

    researchmap

  • 成長円錐のプロテオミクスによるアクチン調節タンパク質の同定

    野住素広, 加藤薫, 五十嵐道弘

    バイオイメージング   15 ( 2 )   45 - 46   2006.10

  • プロテオミクスの手法で同定された成長円錐のアクチン関連蛋白質の網羅的動態観察

    白川彩弓, 戸高玲子, 野住素広, 小澤睦, 五十嵐道弘, 加藤薫

    バイオイメージング   15 ( 2 )   85 - 86   2006.10

  • Proteomics of the growth cone: II. The systematic immunostaining analysis of the growth cone proteins identified by the proteomic research

    Motohiro Nozumi, Michihiro Igarashi

    NEUROSCIENCE RESEARCH   55   S86 - S86   2006

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:ELSEVIER IRELAND LTD  

    Web of Science

    researchmap

  • WAVE/scar proteins control filopodial formation on neuronal growth cones

    M Nozumi, H Nakagawa, H Miki, T Takenawa, S Miyamoto

    MOLECULAR BIOLOGY OF THE CELL   13   58A - 58A   2002.11

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:AMER SOC CELL BIOLOGY  

    Web of Science

    researchmap

▶ display all

Industrial property rights

Research Projects

▶ display all