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N‐terminal polar amino acids of the C2 insert of nonmuscle myosin II ‐C2 regulate its functional properties
Author(s) -
Saha Shekhar,
Halder Debdatta,
Goswami Swagata,
Jana Siddhartha S.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12446
Subject(s) - mutant , myosin , serine , chemistry , myosin light chain kinase , insert (composites) , biophysics , c terminus , microbiology and biotechnology , biochemistry , amino acid , biology , phosphorylation , gene , materials science , composite material
In this study, we investigated the regions in the alternatively spliced C2 insert of nonmuscle myosin ( NM ) II ‐C conferring unique functional properties to the protein. We used constructs carrying deletions within different regions of C2 in neuronal cells; namely, the polar N terminus, the proline/serine‐rich middle, and the nonpolar C terminus. We compared the wild‐type NM II ‐C2 and deletion mutants with respect to ATP ase activity, coassembly with NM II ‐B, regulation by myosin light‐chain kinase ( MLCK ), and solubility, to determine the C2 region(s) involved in these processes. In addition, we examined the ability of the mutants to rescue the neurite‐shortening phenotype upon NM II ‐C2 knockdown in Neuro‐2a cells. Our data highlight the importance of the polar N terminus in NM II ‐C2 function.