BIOPHYSICAL INTERACTION BETWEEN PHOSPHOLAMBAN AND PROTEIN PHOSPHATASE-1 REGULATORY SUBUNIT GM

Citation
I. Berrebibertrand et al., BIOPHYSICAL INTERACTION BETWEEN PHOSPHOLAMBAN AND PROTEIN PHOSPHATASE-1 REGULATORY SUBUNIT GM, FEBS letters, 439(3), 1998, pp. 224-230
Citations number
32
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
0014-5793
Volume
439
Issue
3
Year of publication
1998
Pages
224 - 230
Database
ISI
SICI code
0014-5793(1998)439:3<224:BIBPAP>2.0.ZU;2-T
Abstract
Regulation of the sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA 2a) depends on the phosphorylation state of phospholamban (PLB), When PLB is phosphorylated, its inhibitory effect towards SERCA 2a is relieved , leading to an enhanced myocardial performance, This process is rever sed by a sarcoplasmic reticulum (SR)-associated type 1 protein phospha tase (PP1) composed of a catalytic subunit PP1C and a regulatory subun it Gill, Human Gill and PLB have been produced in an in vitro transcri ption/translation system and used for co-immunoprecipitation and biose nsor experiments, The detected interaction between the two partners su ggests that cardiac PP1 is targeted to PLB via GM and we believe that this process occurs,vith the identified transmembrane domains of the t no proteins, Thus, the interaction between PLB and GM may represent a specific way to modulate the SR function in human cardiac muscle. (C) 1998 Federation of European Biochemical Societies.