Ader

Andronesi

Asahi

Bers

Bick

Boehr

Brini

Buck

D. G. Mullen

G. Veglia

Gustavsson

Hoshijima

James

K. R. Mote

Karim

M. Gustavsson

MacLennan

MacLENNAN

Moller

N. J. Traaseth

R. Verardi

Religa

Sengupta

T. Gopinath

Toyoshima

Trieber

Vangheluwe

Wegener

Young

English

Significance
          
            The sarcoplasmic reticulum Ca
            2+
            -ATPase (SERCA)/phospholamban complex regulates cardiac muscle contractility by controlling Ca
            2+
            transport from the cytosol to the lumen of the sarcoplasmic reticulum. By mapping the interactions between these two membrane proteins, we found that SERCA function depends on the equilibria between transient conformational states of phospholamban. Phosphorylation of phospholamban shifts the equilibria, enhancing SERCA function. This mechanism explains why tuning phospholamban’s structural dynamics can modulate SERCA function and may aid in designing innovative therapeutic approaches to heart failure.
          </jats:p

Martin Gustavsson

Raffaello Verardi

Daniel G. Mullen

Kaustubh R. Mote

Nathaniel J. Traaseth

Gianluigi Veglia

Crossref

Proceedings of the National Academy of Sciences

Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban

http://www.pnas.org/content/110/43/17338.full.pdf

Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban

Abstract

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