Mammalian nonmuscle myosin II comes in three flavors
Creators
- 1. Department of Biology, University of Pennsylvania, Philadelphia, PA, 19104 (United States)
Description
Highlights: • Nonmuscle myosin II executes numerous mechanical tasks in cells including cytoskeleton organization and cell migration. • Three mammalian nonmuscle myosin II paralogs have distinct kinetic and dynamic properties in vitro and in vivo. • Mammalian nonmuscle myosin II paralogs mix and match their abilities to perform both individual and joint tasks in the cell. Nonmuscle myosin II is an actin-based motor that executes numerous mechanical tasks in cells including spatiotemporal organization of the actin cytoskeleton, adhesion, migration, cytokinesis, tissue remodeling, and membrane trafficking. Nonmuscle myosin II is ubiquitously expressed in mammalian cells as a tissue-specific combination of three paralogs. Recent studies reveal novel specific aspects of their kinetics, intracellular regulation and functions. On the other hand, the three paralogs also can copolymerize and cooperate in cells. Here we review the recent advances from the prospective of how distinct features of the three myosin II paralogs adapt them to perform specialized and joint tasks in the cell.
Availability note (English)
Available from http://dx.doi.org/10.1016/j.bbrc.2018.03.103Additional details
Identifiers
- DOI
- 10.1016/j.bbrc.2018.03.103;
- PII
- S0006291X18305953;
Publishing Information
- Journal Title
- Biochemical and Biophysical Research Communications
- Journal Volume
- 506
- Journal Issue
- 2
- Journal Page Range
- p. 394-402
- ISSN
- 0006-291X
- CODEN
- BBRCA9
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 53044128
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- ACTIN; ANIMAL TISSUES; COPOLYMERS; MICROTUBULES; MYOSIN
- Descriptors DEC
- BODY; CELL CONSTITUENTS; GLOBULINS; ORGANIC COMPOUNDS; ORGANIC POLYMERS; POLYMERS; PROTEINS
Optional Information
- Copyright
- Copyright (c) 2018 Elsevier Inc. All rights reserved.