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@ARTICLE{Risi:857021,
author = {Risi, Cristina and Belknap, Betty and Forgacs-Lonart, Eva
and Harris, Samantha P. and Schröder, Gunnar and White,
Howard D. and Galkin, Vitold E.},
title = {{N}-{T}erminal {D}omains of {C}ardiac {M}yosin {B}inding
{P}rotein {C} {C}ooperatively {A}ctivate the {T}hin
{F}ilament},
journal = {Structure},
volume = {26},
number = {12},
issn = {0969-2126},
address = {Cambridge, Mass.},
publisher = {Cell Press},
reportid = {FZJ-2018-06302},
pages = {1604-1611.e4},
year = {2018},
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.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30270174},
UT = {WOS:000454803300007},
doi = {10.1016/j.str.2018.08.007},
url = {https://juser.fz-juelich.de/record/857021},
}