Characterization of isoform diversity among smooth muscle and nonmuscle myosin heavy chains

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
C A Kelley

Abstract

In the last decade, as a result of molecular cloning and the reverse-transcriptase polymerase chain reaction, numerous isoforms of the contractile protein myosin have been discovered. What lags behind their discovery is knowledge of their functions. This review focuses on some of my recent work on the structure, function and regulation of isoforms of the heavy chain of vertebrate smooth muscle and nonmuscle myosin II. Reference to related work in the field is included where appropriate. The particular isoforms discussed are those that are generated by alternative splicing near the 5' end of the pre-mRNA, resulting in either an insertion or a deletion of a cassette of amino acids near the amino-terminus of the myosin heavy chain (MHC) protein. In both the smooth muscle and nonmuscle MHCs, this splicing occurs in the exact same region, which begins at amino acid 212 in the primary sequence. In the three-dimensional structure of the molecule, these inserts are located near the ATP-binding pocket in a region of the MHC that was not resolved in the crystal structure and therefore is believed to represent a flexible loop. In the smooth muscle MHC, the insertion of seven amino acids in this loop confers a higher enzymatic activity on ...Continue Reading

References

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Citations

Sep 12, 1998·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·G C SieckK A Jones
Aug 12, 2003·Gene·Alejandro LealBernd Rautenstrauss
Sep 26, 2000·American Journal of Physiology. Cell Physiology·P J GallagherV Lindner
Jun 7, 2011·Journal of Muscle Research and Cell Motility·Justin A DecarreauChristopher L Berger

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