4.6 Review

Retromer-mediated endosomal protein sorting: all WASHed up!

Journal

TRENDS IN CELL BIOLOGY
Volume 23, Issue 11, Pages 522-528

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2013.04.010

Keywords

retromer; WASH complex; endosome; sorting; actin; Fam21

Categories

Funding

  1. MRC [G0701444]
  2. ANR [ANR-11 BSV2 014 01]
  3. Mayo Foundation
  4. NIH grant [AI065474]
  5. MRC [G0701444] Funding Source: UKRI
  6. Medical Research Council [G0701444] Funding Source: researchfish

Ask authors/readers for more resources

Endosomal protein sorting governs the fate of many physiologically important proteins involved in a panoply of cellular functions. Recent discoveries have revealed a vital role for endosomally localised branched actin patches in facilitating protein sorting. The formation of the actin patches has been shown to require the function of the WASH complex - the major endosomal actin polymerisation-promoting complex - which stimulates the activity of the ubiquitously expressed Arp2/3 complex. Another key component of the endosomal protein-sorting machinery is the retromer complex. Studies now show that retromer mediates the recruitment of the WASH complex and its regulators to endosomes. In this review, recent progress in understanding the role of the WASH complex along with retromer in endosomal protein sorting is discussed.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available