Ontology highlight
ABSTRACT:
SUBMITTER: Ragusa MJ
PROVIDER: S-EPMC2924587 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Ragusa Michael J MJ Dancheck Barbara B Critton David A DA Nairn Angus C AC Page Rebecca R Peti Wolfgang W
Nature structural & molecular biology 20100321 4
The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets. PP1 associates with >or=200 regulatory proteins to form highly specific holoenzymes. These regulatory proteins target PP1 to its point of action within the cell and prime its enzymatic specificity for particular substrates. However, how they direct PP1's specificity is not understood. Here we show that spinophilin, a neuronal PP1 regulator, is entirely unstructured in its unbound form, and it bi ...[more]