Send to

Choose Destination
Elife. 2017 Mar 31;6. pii: e24126. doi: 10.7554/eLife.24126.

A CDC25 family protein phosphatase gates cargo recognition by the Vps26 retromer subunit.

Author information

Department of Cell Biology, Yale School of Medicine, New Haven, United States.
Department of Molecular Physiology and Biophysics, University of Iowa, Iowa City, United States.


We describe a regulatory mechanism that controls the activity of retromer, an evolutionarily conserved sorting device that orchestrates cargo export from the endosome. A spontaneously arising mutation that activates the yeast (Saccharomyces cerevisiae) CDC25 family phosphatase, Mih1, results in accelerated turnover of a subset of endocytosed plasma membrane proteins due to deficient sorting into a retromer-mediated recycling pathway. Mih1 directly modulates the phosphorylation state of the Vps26 retromer subunit; mutations engineered to mimic these states modulate the binding affinities of Vps26 for a retromer cargo, resulting in corresponding changes in cargo sorting at the endosome. The results suggest that a phosphorylation-based gating mechanism controls cargo selection by yeast retromer, and they establish a functional precedent for CDC25 protein phosphatases that lies outside of their canonical role in regulating cell cycle progression.


CDC25 protein phosphatase; arrestin; biochemistry; cell biology; endosome; retromer

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for eLife Sciences Publications, Ltd Icon for PubMed Central
Loading ...
Support Center