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2017 ; 26
(7
): 1337-1351
Nephropedia Template TP
Protein Sci
2017[Jul]; 26
(7
): 1337-1351
PMID28474792
show ga
For individual cells in tissues to create the diverse forms of biological
organisms, it is necessary that they must reliably sense and generate the correct
forces over the correct distances and directions. There is considerable evidence
that the mechanical aspects of the cellular microenvironment provide critical
physical parameters to be sensed. How proteins sense forces and cellular geometry
to create the correct morphology is not understood in detail but protein
unfolding appears to be a major component in force and displacement sensing.
Thus, the crystallographic structure of a protein domain provides only a starting
point to then analyze what will be the effects of physiological forces through
domain unfolding or catch-bond formation. In this review, we will discuss the
recent studies of cytoskeletal and adhesion proteins that describe protein domain
dynamics. Forces applied to proteins can activate or inhibit enzymes, increase or
decrease protein-protein interactions, activate or inhibit protein substrates,
induce catch bonds and regulate interactions with membranes or nucleic acids.
Further, the dynamics of stretch-relaxation can average forces or movements to
reliably regulate morphogenic movements. In the few cases where single molecule
mechanics are studied under physiological conditions such as titin and talin,
there are rapid cycles of stretch-relaxation that produce mechanosensing signals.
Fortunately, the development of new single molecule and super-resolution imaging
methods enable the analysis of single molecule mechanics in physiologically
relevant conditions. Thus, we feel that stereotypical changes in cell and tissue
shape involve mechanosensing that can be analyzed at the nanometer level to
determine the molecular mechanisms involved.
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