Ontology highlight
ABSTRACT:
SUBMITTER: Krysiak J
PROVIDER: S-EPMC5772059 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Krysiak Judith J Unger Andreas A Beckendorf Lisa L Hamdani Nazha N von Frieling-Salewsky Marion M Redfield Margaret M MM Dos Remedios Cris G CG Sheikh Farah F Gergs Ulrich U Boknik Peter P Linke Wolfgang A WA
Nature communications 20180117 1
Serine/threonine protein phosphatase 5 (PP5) is ubiquitously expressed in eukaryotic cells; however, its function in cardiomyocytes is unknown. Under basal conditions, PP5 is autoinhibited, but enzymatic activity rises upon binding of specific factors, such as the chaperone Hsp90. Here we show that PP5 binds and dephosphorylates the elastic N2B-unique sequence (N2Bus) of titin in cardiomyocytes. Using various binding and phosphorylation tests, cell-culture manipulation, and transgenic mouse hear ...[more]