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  1. Artikel: Syndapin Regulates the RAP-1 GTPase to Control Endocytic Recycling via RHO-1 and Non-Muscle Myosin II.

    Rodriguez-Polanco, Wilmer R / Norris, Anne / Velasco, Agustin B / Gleason, Adenrele M / Grant, Barth D

    bioRxiv : the preprint server for biology

    2023  

    Abstract: After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F- ... ...

    Abstract After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F-BAR and SH3 domain Syndapin/PACSIN-family protein SDPN-1 is required
    Sprache Englisch
    Erscheinungsdatum 2023-02-28
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.02.27.530328
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Syndapin and GTPase RAP-1 control endocytic recycling via RHO-1 and non-muscle myosin II.

    Rodriguez-Polanco, Wilmer R / Norris, Anne / Velasco, Agustin B / Gleason, Adenrele M / Grant, Barth D

    Current biology : CB

    2023  Band 33, Heft 22, Seite(n) 4844–4856.e5

    Abstract: After endocytosis, many plasma membrane components are recycled via membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that Syndapin/PACSIN-family ...

    Abstract After endocytosis, many plasma membrane components are recycled via membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that Syndapin/PACSIN-family protein SDPN-1 is required in vivo for basolateral endocytic recycling in the C. elegans intestine. Here, we document an interaction between the SDPN-1 SH3 domain and a target sequence in PXF-1/PDZ-GEF1/RAPGEF2, a known exchange factor for Rap-GTPases. We found that endogenous mutations engineered into the SDPN-1 SH3 domain, or its binding site in the PXF-1 protein, interfere with recycling in vivo, as does the loss of the PXF-1 target RAP-1. In some contexts, Rap-GTPases negatively regulate RhoA activity, suggesting a potential for Syndapin to regulate RhoA. Our results indicate that in the C. elegans intestine, RHO-1/RhoA is enriched on SDPN-1- and RAP-1-positive endosomes, and the loss of SDPN-1 or RAP-1 elevates RHO-1(GTP) levels on intestinal endosomes. Furthermore, we found that depletion of RHO-1 suppressed sdpn-1 mutant recycling defects, indicating that control of RHO-1 activity is a key mechanism by which SDPN-1 acts to promote endocytic recycling. RHO-1/RhoA is well known for controlling actomyosin contraction cycles, although little is known about the effects of non-muscle myosin II on endosomes. Our analysis found that non-muscle myosin II is enriched on SDPN-1-positive endosomes, with two non-muscle myosin II heavy-chain isoforms acting in apparent opposition. Depletion of nmy-2 inhibited recycling like sdpn-1 mutants, whereas depletion of nmy-1 suppressed sdpn-1 mutant recycling defects, indicating that actomyosin contractility controls recycling endosome function.
    Mesh-Begriff(e) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; GTP Phosphohydrolases/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Actomyosin/metabolism ; Endocytosis/physiology ; Endosomes/metabolism ; Myosin Type II/metabolism
    Chemische Substanzen GTP Phosphohydrolases (EC 3.6.1.-) ; Caenorhabditis elegans Proteins ; Actomyosin (9013-26-7) ; Myosin Type II (EC 3.6.1.-)
    Sprache Englisch
    Erscheinungsdatum 2023-10-12
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2023.09.051
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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