Calcium regulation of myosin-I tension sensing.

Abstract:

:Myo1b is a myosin that is exquisitely sensitive to tension. Its actin-attachment lifetime increases > 50-fold when its working stroke is opposed by 1 pN of force. The long attachment lifetime of myo1b under load raises the question: how are actin attachments that last >50 s in the presence of force regulated? Like most myosins, forces are transmitted to the myo1b motor through a light-chain binding domain that is structurally stabilized by calmodulin, a calcium-binding protein. Thus, we examined the effect of calcium on myo1b motility using ensemble and single-molecule techniques. Calcium accelerates key biochemical transitions on the ATPase pathway, decreases the working-stroke displacement, and greatly reduces the ability of myo1b to sense tension. Thus, calcium provides an effective mechanism for inhibiting motility and terminating long-duration attachments.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Lewis JH,Greenberg MJ,Laakso JM,Shuman H,Ostap EM

doi

10.1016/j.bpj.2012.05.014

subject

Has Abstract

pub_date

2012-06-20 00:00:00

pages

2799-807

issue

12

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(12)00567-X

journal_volume

102

pub_type

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