WASH drives early recycling from macropinosomes and phagosomes to maintain surface phagocytic receptors.

Details

Serval ID
serval:BIB_B84A562CF0C8
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
WASH drives early recycling from macropinosomes and phagosomes to maintain surface phagocytic receptors.
Journal
Proceedings of the National Academy of Sciences of the United States of America
Author(s)
Buckley C.M., Gopaldass N., Bosmani C., Johnston S.A., Soldati T., Insall R.H., King J.S.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Publication state
Published
Issued date
2016
Volume
113
Number
40
Pages
E5906-E5915
Language
english
Abstract
Macropinocytosis is an ancient mechanism that allows cells to harvest nutrients from extracellular media, which also allows immune cells to sample antigens from their surroundings. During macropinosome formation, bulk plasma membrane is internalized with all its integral proteins. It is vital for cells to salvage these proteins before degradation, but the mechanisms for sorting them are not known. Here we describe the evolutionarily conserved recruitment of the WASH (WASP and SCAR homolog) complex to both macropinosomes and phagosomes within a minute of internalization. Using Dictyostelium, we demonstrate that WASH drives protein sorting and recycling from macropinosomes and is thus essential to maintain surface receptor levels and sustain phagocytosis. WASH functionally interacts with the retromer complex at both early and late phases of macropinosome maturation, but mediates recycling via retromer-dependent and -independent pathways. WASH mutants consequently have decreased membrane levels of integrins and other surface proteins. This study reveals an important pathway enabling cells to sustain macropinocytosis without bulk degradation of plasma membrane components.
Keywords
phagocytosis, macropinocytosis, WASH, Dictyostelium, trafficking
Pubmed
Web of science
Open Access
Yes
Create date
03/11/2016 8:13
Last modification date
20/08/2019 15:26
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