Key result
Single α-helical (SAH) domains in myosins unfold at low forces and have a high propensity to refold, acting as constant-force springs that may enable motors to carry cargo in dense actin networks.
May refine actomyosin transport models; leaves open physiological roles in cellular force buffering.
The human genome contains 39 myosin genes, divided up into 12 different classes. The structure, cellular function and biochemical properties of many of these isoforms remain poorly characterized and there is still some controversy as to whether some myosin isoforms are monomers or dimers. Myosin isoforms 6 and 10 contain a stable single α-helical (SAH) domain, situated just after the canonical lever. The SAH domain is stiff enough to be able to lengthen the lever allowing the myosin to take a larger step. In addition, atomic force microscopy and atomistic simulations show that SAH domains unfold at relatively low forces and have a high propensity to refold. These properties are likely to be important for protein function, enabling motors to carry cargo in dense actin networks, and other proteins to remain attached to binding partners in the crowded cell.
No takes yet. Share an insight, caveat, or question.
Batchelor et al. (2015) conducted a review in Myosin structural diversity and SAH domains. Single α-helical (SAH) domains was evaluated. Single α-helical (SAH) domains in myosins unfold at low forces and have a high propensity to refold, acting as constant-force springs that may enable motors to carry cargo in dense actin networks.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: