Phospholamban degradation is induced by phosphorylation-mediated ubiquitination and inhibited by interaction with cardiac type Sarco(endo)plasmic reticulum Ca2+-ATPase-Reference-Cited by-同舟云学术

Phospholamban degradation is induced by phosphorylation-mediated ubiquitination and inhibited by interaction with cardiac type Sarco(endo)plasmic reticulum Ca2+-ATPase

Published:2016-04 Issue:3 Volume:472 Page:523-530
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Nakagawa Takatoshi,Yokoe Shunichi,Asahi Michio

Funder

Japan Society for the Promotion of Science

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference30 articles.

1. Phospholamban: a crucial regulator of cardiac contractility;MacLennan;Nat. Rev. Mol. Cell Biol.,2003

2. Regulation of sarco(endo)plasmic reticulum Ca2+ adenosine triphosphatase by phospholamban and sarcolipin: implication for cardiac hypertrophy and failure;Asahi;Trends Cardiovasc Med.,2003

3. Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP;Asahi;J. Biol. Chem.,2000

4. The regulation of SERCA-type pumps by phospholamban and sarcolipin;MacLennan;Ann. N Y Acad. Sci.,2003

5. Phospholamban ablation by RNA interference increases Ca2+ uptake into rat cardiac myocyte sarcoplasmic reticulum;Watanabe;J. Mol. Cell Cardiol.,2004

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