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  1. Article ; Online: Combinatorial expression of γ-protocadherins regulates synaptic connectivity in the mouse neocortex.

    Zhu, Yi-Jun / Deng, Cai-Yun / Fan, Liu / Wang, Ya-Qian / Zhou, Hui / Xu, Hua-Tai

    eLife

    2024  Volume 12

    Abstract: In the process of synaptic formation, neurons must not only adhere to specific principles when selecting synaptic partners but also possess mechanisms to avoid undesirable connections. Yet, the strategies employed to prevent unwarranted associations have ...

    Abstract In the process of synaptic formation, neurons must not only adhere to specific principles when selecting synaptic partners but also possess mechanisms to avoid undesirable connections. Yet, the strategies employed to prevent unwarranted associations have remained largely unknown. In our study, we have identified the pivotal role of combinatorial clustered protocadherin gamma (γ-PCDH) expression in orchestrating synaptic connectivity in the mouse neocortex. Through 5' end single-cell sequencing, we unveiled the intricate combinatorial expression patterns of γ-PCDH variable isoforms within neocortical neurons. Furthermore, our whole-cell patch-clamp recordings demonstrated that as the similarity in this combinatorial pattern among neurons increased, their synaptic connectivity decreased. Our findings elucidate a sophisticated molecular mechanism governing the construction of neural networks in the mouse neocortex.
    MeSH term(s) Animals ; Mice ; Cadherin Related Proteins ; Cadherins/genetics ; Neocortex ; Neural Networks, Computer
    Chemical Substances Gamma-protocadherins ; Cadherin Related Proteins ; Cadherins
    Language English
    Publishing date 2024-03-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.89532
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: JIP1 mediates anterograde transport of Rab10 cargos during neuronal polarization.

    Deng, Cai-Yun / Lei, Wen-Liang / Xu, Xiao-Hui / Ju, Xiang-Chun / Liu, Yang / Luo, Zhen-Ge

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2014  Volume 34, Issue 5, Page(s) 1710–1723

    Abstract: Axon development and elongation require strictly controlled new membrane addition. Previously, we have shown the involvement of Rab10 in directional membrane insertion of plasmalemmal precursor vesicles (PPVs) during neuronal polarization and axonal ... ...

    Abstract Axon development and elongation require strictly controlled new membrane addition. Previously, we have shown the involvement of Rab10 in directional membrane insertion of plasmalemmal precursor vesicles (PPVs) during neuronal polarization and axonal growth. However, the mechanism responsible for PPV transportation remains unclear. Here we show that c-Jun N-terminal kinase-interacting protein 1 (JIP1) interacts with GTP-locked active form of Rab10 and directly connects Rab10 to kinesin-1 light chain (KLC). The kinesin-1/JIP1/Rab10 complex is required for anterograde transport of PPVs during axonal growth. Downregulation of JIP1 or KLC or disrupting the formation of this complex reduces anterograde transport of PPVs in developing axons and causes neuronal polarity defect. Furthermore, this complex plays an important role in neocortical neuronal polarization of rats in vivo. Thus, this study has demonstrated a mechanism underlying directional membrane trafficking involved in axon development.
    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Axons/metabolism ; Brain/cytology ; Cell Polarity/physiology ; Cells, Cultured ; Cellular Structures/metabolism ; Embryo, Mammalian ; Female ; Gene Expression Regulation/physiology ; Humans ; Ki-67 Antigen/metabolism ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Male ; Microscopy, Confocal ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Neurons/cytology ; Neurons/physiology ; Protein Transport/physiology ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Rats ; Rats, Sprague-Dawley ; T-Box Domain Proteins/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Ki-67 Antigen ; Luminescent Proteins ; Mapk8ip1 protein, rat ; Microtubule-Associated Proteins ; RNA, Small Interfering ; Rab10 protein, rat ; T-Box Domain Proteins ; kinesin light-chain proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-01-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.4496-13.2014
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    Zs.A 1668: Show issues Location:
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  3. Article ; Online: Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development.

    Liu, Yang / Xu, Xiao-Hui / Chen, Qi / Wang, Tong / Deng, Cai-Yun / Song, Bao-Liang / Du, Jiu-Lin / Luo, Zhen-Ge

    Nature communications

    2013  Volume 4, Page(s) 2005

    Abstract: Polarized membrane addition is crucial for axon development and elongation during neuronal morphogenesis. This process is believed to be regulated by directed membrane trafficking of Rab10-containing post-Golgi carriers. However, the mechanisms ... ...

    Abstract Polarized membrane addition is crucial for axon development and elongation during neuronal morphogenesis. This process is believed to be regulated by directed membrane trafficking of Rab10-containing post-Golgi carriers. However, the mechanisms underlying the biogenesis of these carriers remain unclear. Here, we report that Rab10 interaction with myosin Vb (MYO5B) determines the formation of Rab10 carriers and is important for axon development. Rab10 interacts with the exon D-encoded domain of MYO5B. Downregulating the expression of MYO5B (+D) or blocking its interaction with Rab10 impairs the fission of Rab10 vesicles from trans-Golgi membranes, causes a decrease in the number of Rab10 transport carriers and inhibits axon development in cultured hippocampal neurons. Furthermore, the MYO5B-Rab10 system is required for axon development of vertebrate neocortical neurons or zebrafish retinal ganglion cells in vivo. Thus, specific interaction between Rab10 and MYO5B controls the formation of Rab10 vesicles, which is required for axon development.
    MeSH term(s) Amino Acid Sequence ; Animals ; Axons/drug effects ; Axons/metabolism ; Axons/ultrastructure ; Cell Polarity/drug effects ; Exons/genetics ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Golgi Apparatus/drug effects ; Golgi Apparatus/metabolism ; Guanosine Triphosphate/metabolism ; HEK293 Cells ; Hippocampus/cytology ; Humans ; Molecular Sequence Data ; Morpholinos/pharmacology ; Myosins/chemistry ; Myosins/metabolism ; Optic Nerve/drug effects ; Optic Nerve/growth & development ; Optic Nerve/metabolism ; Protein Binding/drug effects ; RNA, Small Interfering/metabolism ; Rats ; Retinal Ganglion Cells/cytology ; Retinal Ganglion Cells/drug effects ; Retinal Ganglion Cells/metabolism ; Transport Vesicles/drug effects ; Transport Vesicles/metabolism ; Transport Vesicles/ultrastructure ; Zebrafish ; Zebrafish Proteins/chemistry ; Zebrafish Proteins/metabolism ; rab GTP-Binding Proteins/metabolism ; trans-Golgi Network/drug effects ; trans-Golgi Network/metabolism
    Chemical Substances Morpholinos ; Myo5b protein, rat ; RNA, Small Interfering ; Rab10 protein, rat ; Zebrafish Proteins ; Guanosine Triphosphate (86-01-1) ; Myosins (EC 3.6.4.1) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2013
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/ncomms3005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Laminin/β1 integrin signal triggers axon formation by promoting microtubule assembly and stabilization.

    Lei, Wen-Liang / Xing, Shi-Ge / Deng, Cai-Yun / Ju, Xiang-Chun / Jiang, Xing-Yu / Luo, Zhen-Ge

    Cell research

    2012  Volume 22, Issue 6, Page(s) 954–972

    Abstract: Axon specification during neuronal polarization is closely associated with increased microtubule stabilization in one of the neurites of unpolarized neuron, but how this increased microtubule stability is achieved is unclear. Here, we show that ... ...

    Abstract Axon specification during neuronal polarization is closely associated with increased microtubule stabilization in one of the neurites of unpolarized neuron, but how this increased microtubule stability is achieved is unclear. Here, we show that extracellular matrix (ECM) component laminin promotes neuronal polarization via regulating directional microtubule assembly through β1 integrin (Itgb1). Contact with laminin coated on culture substrate or polystyrene beads was sufficient for axon specification of undifferentiated neurites in cultured hippocampal neurons and cortical slices. Active Itgb1 was found to be concentrated in laminin-contacting neurites. Axon formation was promoted and abolished by enhancing and attenuating Itgb1 signaling, respectively. Interestingly, laminin contact promoted plus-end microtubule assembly in a manner that required Itgb1. Moreover, stabilizing microtubules partially prevented polarization defects caused by Itgb1 downregulation. Finally, genetic ablation of Itgb1 in dorsal telencephalic progenitors caused deficits in axon development of cortical pyramidal neurons. Thus, laminin/Itgb1 signaling plays an instructive role in axon initiation and growth, both in vitro and in vivo, through the regulation of microtubule assembly. This study has established a linkage between an extrinsic factor and intrinsic cytoskeletal dynamics during neuronal polarization.
    MeSH term(s) Animals ; Axons/physiology ; Cells, Cultured ; Down-Regulation ; HEK293 Cells ; Hippocampus/cytology ; Hippocampus/metabolism ; Humans ; Integrin beta1/chemistry ; Integrin beta1/genetics ; Integrin beta1/metabolism ; Laminin/antagonists & inhibitors ; Laminin/genetics ; Laminin/metabolism ; Mice ; Mice, Knockout ; Microtubules/physiology ; Neurites/metabolism ; Neurons/cytology ; Neurons/metabolism ; Polystyrenes/chemistry ; Protein-Serine-Threonine Kinases/metabolism ; RNA Interference ; RNA, Small Interfering ; Signal Transduction
    Chemical Substances Integrin beta1 ; Laminin ; Polystyrenes ; RNA, Small Interfering ; Stk11 protein, mouse (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2012-03-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/cr.2012.40
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5283: Show issues Location:
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  5. Article ; Online: MARCKS regulates membrane targeting of Rab10 vesicles to promote axon development.

    Xu, Xiao-Hui / Deng, Cai-Yun / Liu, Yang / He, Miao / Peng, Jian / Wang, Tong / Yuan, Lei / Zheng, Zhi-Sheng / Blackshear, Perry J / Luo, Zhen-Ge

    Cell research

    2014  Volume 24, Issue 5, Page(s) 576–594

    Abstract: Axon development requires membrane addition from the intracellular supply, which has been shown to be mediated by Rab10-positive plasmalemmal precursor vesicles (PPVs). However, the molecular mechanisms underlying the membrane trafficking processes of ... ...

    Abstract Axon development requires membrane addition from the intracellular supply, which has been shown to be mediated by Rab10-positive plasmalemmal precursor vesicles (PPVs). However, the molecular mechanisms underlying the membrane trafficking processes of PPVs remain unclear. Here, we show that myristoylated alanine-rich C-kinase substrate (MARCKS) mediates membrane targeting of Rab10-positive PPVs, and this regulation is critical for axon development. We found that the GTP-locked active form of Rab10 binds to membrane-associated MARCKS, whose affinity depends on the phosphorylation status of the MARCKS effector domain. Either genetic silencing of MARCKS or disruption of its interaction with Rab10 inhibited axon growth of cortical neurons, impaired docking and fusion of Rab10 vesicles with the plasma membrane, and consequently caused a loss of membrane insertion of axonal receptors responsive to extracellular axon growth factors. Thus, this study has identified a novel function of MARCKS in mediating membrane targeting of PPVs during axon development.
    MeSH term(s) Actins/metabolism ; Animals ; Axons/metabolism ; Axons/ultrastructure ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Cells, Cultured ; Humans ; Intracellular Signaling Peptides and Proteins/analysis ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Fusion ; Membrane Proteins/analysis ; Membrane Proteins/metabolism ; Myristoylated Alanine-Rich C Kinase Substrate ; Neurons/cytology ; Neurons/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Rats ; rab GTP-Binding Proteins/analysis ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Actins ; Intracellular Signaling Peptides and Proteins ; MARCKS protein, human ; Marcks protein, rat ; Membrane Proteins ; Rab10 protein, rat ; Myristoylated Alanine-Rich C Kinase Substrate (125267-21-2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-03-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/cr.2014.33
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  6. Article: Lgl1 Activation of Rab10 Promotes Axonal Membrane Trafficking Underlying Neuronal Polarization

    Wang, Tong / Liu, Yang / Xu, Xiao-Hui / Deng, Cai-Yun / Wu, Kong-Yan / Zhu, Ji / Fu, Xiu-Qing / He, Miao / Luo, Zhen-Ge

    Developmental cell. 2011 Sept. 13, v. 21, no. 3

    2011  

    Abstract: Directed membrane trafficking is believed to be crucial for axon development during neuronal morphogenesis. However, the underlying mechanisms are poorly understood. Here, we report a role of Lgl1, the mammalian homolog of Drosophila tumor suppressor ... ...

    Abstract Directed membrane trafficking is believed to be crucial for axon development during neuronal morphogenesis. However, the underlying mechanisms are poorly understood. Here, we report a role of Lgl1, the mammalian homolog of Drosophila tumor suppressor Lethal giant larvae, in controlling membrane trafficking underlying axonal growth. We find that Lgl1 is associated with plasmalemmal precursor vesicles and enriched in developing axons. Lgl1 upregulation promoted axonal growth, whereas downregulation attenuated it as well as directional membrane insertion. Interestingly, Lgl1 interacted with and activated Rab10, a small GTPase that mediates membrane protein trafficking, by releasing GDP dissociation inhibitor (GDI) from Rab10. Furthermore, Rab10 lies downstream of Lgl1 in axon development and directional membrane insertion. Finally, both Lgl1 and Rab10 are required for neocortical neuronal polarization in vivo. Thus, the Lgl1 regulation of Rab10 stimulates the trafficking of membrane precursor vesicles, whose fusion with the plasmalemma is crucial for axonal growth.
    Keywords Drosophila ; axons ; dissociation ; guanosinetriphosphatase ; larvae ; mammals ; membrane proteins ; morphogenesis ; plasma membrane ; protein transport
    Language English
    Dates of publication 2011-0913
    Size p. 431-444.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2011.07.007
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Lgl1 activation of rab10 promotes axonal membrane trafficking underlying neuronal polarization.

    Wang, Tong / Liu, Yang / Xu, Xiao-Hui / Deng, Cai-Yun / Wu, Kong-Yan / Zhu, Ji / Fu, Xiu-Qing / He, Miao / Luo, Zhen-Ge

    Developmental cell

    2011  Volume 21, Issue 3, Page(s) 431–444

    Abstract: Directed membrane trafficking is believed to be crucial for axon development during neuronal morphogenesis. However, the underlying mechanisms are poorly understood. Here, we report a role of Lgl1, the mammalian homolog of Drosophila tumor suppressor ... ...

    Abstract Directed membrane trafficking is believed to be crucial for axon development during neuronal morphogenesis. However, the underlying mechanisms are poorly understood. Here, we report a role of Lgl1, the mammalian homolog of Drosophila tumor suppressor Lethal giant larvae, in controlling membrane trafficking underlying axonal growth. We find that Lgl1 is associated with plasmalemmal precursor vesicles and enriched in developing axons. Lgl1 upregulation promoted axonal growth, whereas downregulation attenuated it as well as directional membrane insertion. Interestingly, Lgl1 interacted with and activated Rab10, a small GTPase that mediates membrane protein trafficking, by releasing GDP dissociation inhibitor (GDI) from Rab10. Furthermore, Rab10 lies downstream of Lgl1 in axon development and directional membrane insertion. Finally, both Lgl1 and Rab10 are required for neocortical neuronal polarization in vivo. Thus, the Lgl1 regulation of Rab10 stimulates the trafficking of membrane precursor vesicles, whose fusion with the plasmalemma is crucial for axonal growth.
    MeSH term(s) Animals ; Axons/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Polarity ; Cells, Cultured ; Down-Regulation ; Guanine Nucleotide Dissociation Inhibitors/metabolism ; Hippocampus/growth & development ; Hippocampus/metabolism ; Humans ; Protein Transport ; Proteins/metabolism ; Rats ; Up-Regulation ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Guanine Nucleotide Dissociation Inhibitors ; LGL1 protein, rat ; Proteins ; Rab10 protein, rat ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2011-09-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2011.07.007
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    Zs.A 5742: Show issues Location:
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