Journal Article

FZJ-2018-06302

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament

Risi, C. ; Belknap, B. ; Forgacs-Lonart, E. ; Harris, S. P. ; Schröder, G.FZJ* ; White, H. D. ; Galkin, V. E. (Corresponding author)

2018
Cell Press Cambridge, Mass.

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Please use a persistent id in citations: doi:10.1016/j.str.2018.08.007

Abstract: Muscle contraction relies on interaction betweenmyosin-based thick filaments and actin-based thinfilaments. Myosin binding protein C (MyBP-C) is akey regulator of actomyosin interactions. Recentstudies established that the N0-terminal domains(NTDs) of MyBP-C can either activate or inhibit thinfilaments, but the mechanism of their collectiveaction is poorly understood. Cardiac MyBP-C(cMyBP-C) harbors an extra NTD, which is absentin skeletal isoforms of MyBP-C, and its role in regulationof cardiac contraction is unknown. Here weshow that the first two domains of human cMyPB-C(i.e., C0 and C1) cooperate to activate the thin filament.We demonstrate that C1 interacts with tropomyosinvia a positively charged loop and that thisinteraction, stabilized by the C0 domain, is requiredfor thin filament activation by cMyBP-C. Our datareveal a mechanism by which cMyBP-C can modulatecardiac contraction and demonstrate a function of the C0 domain.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2018

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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