Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae
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Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAINThe myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive mannerDistinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cyclingIn the thick of it: HCM-causing mutations in myosin binding proteins of the thick filamentDetermination of the critical residues responsible for cardiac myosin binding protein C's interactionsC0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.The A31P missense mutation in cardiac myosin binding protein C alters protein structure but does not cause haploinsufficiency.Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerMyosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cellsProtein kinase A changes calcium sensitivity but not crossbridge kinetics in human cardiac myofibrils.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-CCardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin.Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C.Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Myofilaments: Movers and Rulers of the Sarcomere.Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein CMYBPC3 mutations are associated with a reduced super-relaxed state in patients with hypertrophic cardiomyopathy.Cardiac myosin binding protein C and its phosphorylation regulate multiple steps in the cross-bridge cycle of muscle contraction.Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Modulation of thin filament activation of myosin ATP hydrolysis by N-terminal domains of cardiac myosin binding protein-C.Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner.
P2860
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P2860
Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
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name
Contribution of the myosin bin ...... n permeabilized rat trabeculae
@en
type
label
Contribution of the myosin bin ...... n permeabilized rat trabeculae
@en
prefLabel
Contribution of the myosin bin ...... n permeabilized rat trabeculae
@en
P2093
P2860
P356
P1476
Contribution of the myosin bin ...... n permeabilized rat trabeculae
@en
P2093
Kristina L Bezold
Maria V Razumova
Michael Regnier
Samantha P Harris
P2860
P304
P356
10.1085/JGP.200810013
P577
2008-11-01T00:00:00Z