Open AccessRegulation of MST complexes and activity via SARAH domain modifications
Author(s) -
Sofiia Karchugina,
Dorothy Benton,
Jonathan Chernoff
Publication year - 2021
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20200559
Subject(s) - hippo signaling pathway , phosphorylation , suppressor , domain (mathematical analysis) , association (psychology) , c terminus , ww domain , microbiology and biotechnology , chemistry , biology , computational biology , signal transduction , genetics , amino acid , philosophy , gene , mathematical analysis , mathematics , epistemology
Three elements of the Hippo tumor suppressor pathway - MST1/2, SAV1, and RASSF1-6 - share in common a C-terminal interaction motif termed the SARAH domain. Proteins containing this domain are capable of self-association as homodimers and also of trans-association with other SARAH domain containing proteins as well as selected additional proteins that lack this domain. Recently, the association of MST1/2 with itself or with other proteins has been shown to be regulated by phosphorylation at sites near or within the SARAH domain. In this review, we focus on recent findings regarding the regulation of such MST1/2 interactions, with an emphasis on the effects of these events on Hippo pathway activity.