Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites
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Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs)A mutation in the human phospholamban gene, deleting arginine 14, results in lethal, hereditary cardiomyopathy.What the structure of a calcium pump tells us about its mechanismModeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPasesSarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholambanIon pathways in the sarcoplasmic reticulum Ca2+-ATPaseThe Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic ReticulumThe sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasmCardiac-specific overexpression of sarcolipin inhibits sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA2a) activity and impairs cardiac function in miceA peptide encoded by a transcript annotated as long noncoding RNA enhances SERCA activity in muscleLocating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopySarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (review).Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.Cardiac-specific overexpression of sarcolipin in phospholamban null mice impairs myocyte function that is restored by phosphorylationHuman phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human.Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Atomic-level mechanisms for phospholamban regulation of the calcium pump.Identification of Small Ankyrin 1 as a Novel Sarco(endo)plasmic Reticulum Ca2+-ATPase 1 (SERCA1) Regulatory Protein in Skeletal Muscle.Post-translational protein modification by O-linked N-acetyl-glucosamine: its role in mediating the adverse effects of diabetes on the heart.Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump.The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival.Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.Calcium pumps in health and disease.Sarcoplasmic reticulum function in smooth muscle.Sarcolipin retention in the endoplasmic reticulum depends on its C-terminal RSYQY sequence and its interaction with sarco(endo)plasmic Ca(2+)-ATPases.The Ca2+ pumps of the endoplasmic reticulum and Golgi apparatus.Direct activation of gastric H,K-ATPase by N-terminal protein kinase C phosphorylation. Comparison of the acute regulation mechanisms of H,K-ATPase and Na,K-ATPase.HSP70 binds to the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ -ATPase (SERCA1a) and prevents thermal inactivation.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.Istaroxime stimulates SERCA2a and accelerates calcium cycling in heart failure by relieving phospholamban inhibition.Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase.Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.Role of leucine 31 of phospholamban in structural and functional interactions with the Ca2+ pump of cardiac sarcoplasmic reticulum.Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.Interactions between small ankyrin 1 and sarcolipin coordinately regulate activity of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1).Polymorphic ventricular tachycardia and abnormal Ca2+ handling in very-long-chain acyl-CoA dehydrogenase null miceSolid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayersSolid-state NMR reveals structural changes in phospholamban accompanying the functional regulation of Ca2+-ATPase
P2860
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P2860
Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Transmembrane helix M6 in sarc ...... al interactions at other sites
@ast
Transmembrane helix M6 in sarc ...... al interactions at other sites
@en
Transmembrane helix M6 in sarc ...... al interactions at other sites
@nl
type
label
Transmembrane helix M6 in sarc ...... al interactions at other sites
@ast
Transmembrane helix M6 in sarc ...... al interactions at other sites
@en
Transmembrane helix M6 in sarc ...... al interactions at other sites
@nl
prefLabel
Transmembrane helix M6 in sarc ...... al interactions at other sites
@ast
Transmembrane helix M6 in sarc ...... al interactions at other sites
@en
Transmembrane helix M6 in sarc ...... al interactions at other sites
@nl
P2093
P2860
P356
P1476
Transmembrane helix M6 in sarc ...... al interactions at other sites
@en
P2093
P2860
P304
P356
10.1074/JBC.274.46.32855
P407
P577
1999-11-12T00:00:00Z