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ASPPs multimerize protein phosphatase 1
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DOI：10.1371/journal.pgen.1011731.png)
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Abstract
En 中文
Protein Phosphatase 1 (PP1) activity is thought to be spatiotemporally defined by hundreds of different regulatory subunits, but their mechanisms of action are largely unknown. The Ankyrin repeat, SH3-domain, and Proline-rich region containing Proteins (ASPPs) bind and localize PP1 to cell-cell junctions. Here, we show ASPPs bind superstoichiometric amounts of PP1. Missense mutations in the ankyrin repeats of ASPPs, that were previously isolated from a forward genetic screen in Caenorhabditis elegans, reduce the stoichiometry of PP1 binding. Forcing PP1 oligomerization restores mutant ASPP function in vivo. We propose that ASPPs multimerize PP1 to establish a concentrated hub of phosphatase activity at cell-cell junctions.
Keywords:
APOPTOSIS-STIMULATING PROTEIN
TUMOR-SUPPRESSOR
P53
CARDIOMYOPATHY
IASPP
BINDING
PHOSPHORYLATION
INHIBITOR
MOLECULES
INTERACTS
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