Distinct sites in tropomyosin specify shared and isoform-specific regulation of myosins II and V

Author:

Barua Bipasha1,Sckolnick Maria2,White Howard D.3,Trybus Kathleen M.2,Hitchcock-DeGregori Sarah E.1

Affiliation:

1. Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School; Rutgers University; Piscataway New Jersey 08854

2. Department of Molecular Physiology; Biophysics University of Vermont; Burlington Vermont 05405

3. Department of Physiological Sciences; Eastern Virginia Medical School; Norfolk Virginia 23507

Funder

National Institutes of Health

American Heart Association

Publisher

Wiley

Subject

Cell Biology,Structural Biology

Reference90 articles.

1. Myosin-Va contributes to manifestation of malignant-related properties in melanoma cells;Alves;Journal of Investigative Dermatology,2013

2. Full-length myosin Va exhibits altered gating during processive movement on actin;Armstrong;Proceedings of the National Academy of Sciences of the United States of America,2012

3. A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin;Barua;The Journal of Biological Chemistry,2013

4. Regulation of nonmuscle myosin II by tropomyosin;Barua;Biochemistry,2014

5. Evolutionarily conserved surface residues constitute actin binding sites of tropomyosin;Barua;Proceedings of the National Academy of Sciences of the United States of America,2011

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