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SWIP mediates retromer-independent membrane recruitment of the WASH complex

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F23%3A10462127" target="_blank" >RIV/00216208:11310/23:10462127 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=w_VypCkIwn" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=w_VypCkIwn</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1111/tra.12884" target="_blank" >10.1111/tra.12884</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    SWIP mediates retromer-independent membrane recruitment of the WASH complex

  • Original language description

    The pentameric WASH complex facilitates endosomal protein sorting by activating Arp2/3, which in turn leads to the formation of F-actin patches specifically on the endosomal surface. It is generally accepted that WASH complex attaches to the endosomal membrane via the interaction of its subunit FAM21 with the retromer subunit VPS35. However, we observe the WASH complex and F-actin present on endosomes even in the absence of VPS35. We show that the WASH complex binds to the endosomal surface in both a retromer-dependent and a retromer-independent manner. The retromer-independent membrane anchor is directly mediated by the subunit SWIP. Furthermore, SWIP can interact with a number of phosphoinositide species. Of those, our data suggest that the interaction with phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2) is crucial to the endosomal binding of SWIP. Overall, this study reveals a new role of the WASH complex subunit SWIP and highlights the WASH complex as an independent, self-sufficient trafficking regulator.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10600 - Biological sciences

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Traffic

  • ISSN

    1398-9219

  • e-ISSN

    1600-0854

  • Volume of the periodical

    24

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    DK - DENMARK

  • Number of pages

    15

  • Pages from-to

    216-230

  • UT code for WoS article

    000962246200001

  • EID of the result in the Scopus database

    2-s2.0-85151930452