Vps3 and Vps8 control integrin trafficking from early to recycling endosomes and regulate integrin-dependent functions

Caspar T. H. Jonker, Romain Galmes, Tineke Veenendaal, Corlinda Brink, Reini E. N. Welle, Nalan Liv, Johan Rooij, Andrew A. Peden, Peter van der Sluijs, Coert Margadant and Judith Klumperman ()
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Caspar T. H. Jonker: Utrecht University
Romain Galmes: Utrecht University
Tineke Veenendaal: Utrecht University
Corlinda Brink: Utrecht University
Reini E. N. Welle: Utrecht University
Nalan Liv: Utrecht University
Johan Rooij: Utrecht Universty
Andrew A. Peden: The University of Sheffield
Peter van der Sluijs: Utrecht University
Coert Margadant: Sanquin Research
Judith Klumperman: Utrecht University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract Recycling endosomes maintain plasma membrane homeostasis and are important for cell polarity, migration, and cytokinesis. Yet, the molecular machineries that drive endocytic recycling remain largely unclear. The CORVET complex is a multi-subunit tether required for fusion between early endosomes. Here we show that the CORVET-specific subunits Vps3 and Vps8 also regulate vesicular transport from early to recycling endosomes. Vps3 and Vps8 localise to Rab4-positive recycling vesicles and co-localise with the CHEVI complex on Rab11-positive recycling endosomes. Depletion of Vps3 or Vps8 does not affect transferrin recycling, but delays the delivery of internalised integrins to recycling endosomes and their subsequent return to the plasma membrane. Consequently, Vps3/8 depletion results in defects in integrin-dependent cell adhesion and spreading, focal adhesion formation, and cell migration. These data reveal a role for Vps3 and Vps8 in a specialised recycling pathway important for integrin trafficking.

Date: 2018
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DOI: 10.1038/s41467-018-03226-8

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