Publication Date:
2008-07-05
Description:
The ability to sense molecular tension is crucial for a wide array of cellular processes, including the detection of auditory stimuli, control of cell shape, and internalization and transport of membranes. We show that myosin I, a motor protein that has been implicated in powering key steps in these processes, dramatically alters its motile properties in response to tension. We measured the displacement generated by single myosin I molecules, and we determined the actin-attachment kinetics with varying tensions using an optical trap. The rate of myosin I detachment from actin decreases 〉75-fold under tension of 2 piconewtons or less, resulting in myosin I transitioning from a low (〈0.2) to a high (〉0.9) duty-ratio motor. This impressive tension sensitivity supports a role for myosin I as a molecular force sensor.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2493443/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2493443/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laakso, Joseph M -- Lewis, John H -- Shuman, Henry -- Ostap, E Michael -- AR051174/AR/NIAMS NIH HHS/ -- GM057247/GM/NIGMS NIH HHS/ -- P01 AR051174/AR/NIAMS NIH HHS/ -- P01 AR051174-050003/AR/NIAMS NIH HHS/ -- R01 GM057247-10/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Jul 4;321(5885):133-6. doi: 10.1126/science.1159419.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18599791" target="_blank"〉PubMed〈/a〉
Keywords:
Actins/*metabolism
;
Actomyosin/physiology
;
Adenosine Diphosphate/metabolism
;
Adenosine Triphosphate/metabolism
;
Amino Acid Motifs
;
Animals
;
Biophysical Phenomena
;
Biophysics
;
Kinetics
;
Likelihood Functions
;
Models, Biological
;
Molecular Motor Proteins/metabolism/*physiology
;
Monte Carlo Method
;
Myosin Type I/chemistry/metabolism/*physiology
;
Optical Tweezers
;
Protein Structure, Tertiary
;
Rabbits
;
Stress, Mechanical
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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