Premium
Four things to know about myosin light chains as reporters for non‐muscle myosin‐2 dynamics in live cells
Author(s) -
Heissler Sarah M.,
Sellers James R.
Publication year - 2015
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21212
Subject(s) - myosin , biology , myosin light chain kinase , actin , microbiology and biotechnology , meromyosin , myosin head , myh7 , myofilament , cytoplasm , function (biology) , biochemistry , myocyte , biophysics
The interplay between non‐muscle myosins‐2 and filamentous actin results in cytoplasmic contractility which is essential for eukaryotic life. Concomitantly, there is tremendous interest in elucidating the physiological function and temporal localization of non‐muscle myosin‐2 in cells. A commonly used method to study the function and localization of non‐muscle myosin‐2 is to overexpress a fluorescent protein (FP)‐tagged version of the regulatory light chain (RLC) which binds to the myosin‐2 heavy chain by mass action. Caveats about this approach include findings from recent studies indicating that the RLC does not bind exclusively to the non‐muscle myosin‐2 heavy chain. Rather, it can also associate with the myosin heavy chains of several other classes as well as other targets than myosin. In addition, the presence of the FP moiety may compromise myosin's enzymatic and mechanical performance. This and other factors to be discussed in this commentary raise questions about the possible complications in using FP‐RLC as a marker for the dynamic localization and regulatory aspects of non‐muscle myosin‐2 motor functions in cell biological experiments. Published 2015. This article is a U.S. Government work and is in the public domain in the USA.