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Control of myosin-I force sensing by alternative splicing.

Authors: Laakso, JM  Lewis, JH  Shuman, H  Ostap, EM 
Citation: Laakso JM, etal., Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):698-702. doi: 10.1073/pnas.0911426107. Epub 2009 Dec 22.
Pubmed: (View Article at PubMed) PMID:20080738
DOI: Full-text: DOI:10.1073/pnas.0911426107

Myosin-Is are molecular motors that link cellular membranes to the actin cytoskeleton, where they play roles in mechano-signal transduction and membrane trafficking. Some myosin-Is are proposed to act as force sensors, dynamically modulating their motile properties in response to changes in tension. In this study, we examined force sensing by the widely expressed myosin-I isoform, myo1b, which is alternatively spliced in its light chain binding domain (LCBD), yielding proteins with lever arms of different lengths. We found the actin-detachment kinetics of the splice isoforms to be extraordinarily tension-sensitive, with the magnitude of tension sensitivity to be related to LCBD splicing. Thus, in addition to regulating step-size, motility rates, and myosin activation, the LCBD is a key regulator of force sensing. We also found that myo1b is substantially more tension-sensitive than other myosins with similar length lever arms, indicating that different myosins have different tension-sensitive transitions.


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CRRD Object Information
CRRD ID: 8554448
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.