Activity of a ubiquitin ligase adaptor is regulated by disordered insertions in its arrestin domain.

Abstract:

:The protein composition of the plasma membrane is rapidly remodeled in response to changes in nutrient availability or cellular stress. This occurs, in part, through the selective ubiquitylation and endocytosis of plasma membrane proteins, which in the yeast Saccharomyces cerevisiae is mediated by the HECT E3 ubiquitin ligase Rsp5 and arrestin--related trafficking (ART) adaptors. Here, we provide evidence that the ART protein family members are composed of an arrestin fold with interspersed disordered loops. Using Art1 as a model, we show that these loop and tail regions, while not strictly required for function, regulate its activity through two separate mechanisms. Disruption of one loop mediates Art1 substrate specificity. Other loops are subjected to phosphorylation in a manner dependent on the Pho85 cyclins Clg1 and Pho80. Phosphorylation of the loops controls Art1's localization to the plasma membrane, which promotes cargo ubiquitylation and endocytosis, demonstrating a mechanism through which Art1 activity is regulated.

journal_name

Mol Biol Cell

authors

Baile MG,Guiney EL,Sanford EJ,MacGurn JA,Smolka MB,Emr SD

doi

10.1091/mbc.E19-08-0451

subject

Has Abstract

pub_date

2019-12-01 00:00:00

pages

3057-3072

issue

25

eissn

1059-1524

issn

1939-4586

journal_volume

30

pub_type

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