TY - JOUR
T1 - Molecular Paradigms for Biological Mechanosensing
AU - Gomez, David
AU - Peña Ccoa, Willmor J.
AU - Singh, Yuvraj
AU - Rojas, Enrique
AU - Hocky, Glen M.
N1 - Funding Information:
G.M.H. would like to thank many colleagues for helpful conversations, including, in particular, members of the Dinner, Gardel, Kovar, and Voth groups (University of Chicago), and the De La Cruz lab (Yale) for past collaborations on mechanosensing in the actin cytoskeleton. Dr. Michael Hartmann was crucial to the development of FISST and to preliminary studies of activation of GPR68. G.M.H. would like to thank Martin McCullagh and group (Oklahoma State) for past collaboration and discussion on allostery. We thank Juan Vanegas (Vermont) for insightful discussions and aid in setting up MscL channel activation simulations. We thank New York University for financial support to all authors. G.M.H. thanks the National Institutes of Health for supporting his group’s work into the origins of molecular mechanosensing via Award R35-GM138312, which funds the work of D.G., Y.S., and G.M.H. in this area. E.R. likewise thanks the NIH for supporting his work on mechanical mechanisms of antibiotics via Award R35-GM143057, which also supports D.G. Support for W.J.P.C. was also provided by the Department of Energy via Award DE-SC0019695.
Publisher Copyright:
© 2021 American Chemical Society
PY - 2021/11/11
Y1 - 2021/11/11
N2 - Many proteins in living cells are subject to mechanical forces, which can be generated internally by molecular machines, or externally, e.g., by pressure gradients. In general, these forces fall in the piconewton range, which is similar in magnitude to forces experienced by a molecule due to thermal fluctuations. While we would naively expect such moderate forces to produce only minimal changes, a wide variety of “mechanosensing” proteins have evolved with functions that are responsive to forces in this regime. The goal of this article is to provide a physical chemistry perspective on protein-based molecular mechanosensing paradigms used in living systems, and how these paradigms can be explored using novel computational methods.
AB - Many proteins in living cells are subject to mechanical forces, which can be generated internally by molecular machines, or externally, e.g., by pressure gradients. In general, these forces fall in the piconewton range, which is similar in magnitude to forces experienced by a molecule due to thermal fluctuations. While we would naively expect such moderate forces to produce only minimal changes, a wide variety of “mechanosensing” proteins have evolved with functions that are responsive to forces in this regime. The goal of this article is to provide a physical chemistry perspective on protein-based molecular mechanosensing paradigms used in living systems, and how these paradigms can be explored using novel computational methods.
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U2 - 10.1021/acs.jpcb.1c06330
DO - 10.1021/acs.jpcb.1c06330
M3 - Article
C2 - 34709040
AN - SCOPUS:85118940557
VL - 125
SP - 12115
EP - 12124
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
IS - 44
ER -