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Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB.

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Title: Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB.
Authors: Sato, Masaaki K Browse this author
Takahashi, Masayuki Browse this author →KAKEN DB
Yazawa, Michio Browse this author
Issue Date: Mar-2007
Publisher: The American Society for Cell Biology
Journal Title: Molecular biology of the cell
Volume: 18
Issue: 3
Start Page: 1009
End Page: 1017
Publisher DOI: 10.1091/mbc.E06-08-0706
PMID: 17202408
Abstract: To function in the cell, nonmuscle myosin II molecules assemble into filaments through their C-terminal tails. Because myosin II isoforms most likely assemble into homo-filaments in vivo, it seems that some self-recognition mechanisms of individual myosin II isoforms should exist. Exogenous expression of myosin IIB rod fragment is thus expected to prevent the function of myosin IIB specifically. We expected to reveal some self-recognition sites of myosin IIB from the phenotype by expressing appropriate myosin IIB rod fragments. We expressed the C-terminal 305-residue rod fragment of the myosin IIB heavy chain (BRF305) in MRC-5 SV1 TG1 cells. As a result, unstable morphology was observed like MHC-IIB(-/-) fibroblasts. This phenotype was not observed in cells expressing BRF305 mutants: 1) with a defect in assembling, 2) lacking N-terminal 57 residues (N-57), or 3) lacking C-terminal 63 residues (C-63). A myosin IIA rod fragment ARF296 corresponding to BRF305 was not effective. However, the chimeric ARF296, in which the N-57 and C-63 of BRF305 were substituted for the corresponding regions of ARF296, acquired the ability to induce unstable morphology. We propose that the N-57 and C-63 of BRF305 are involved in self-recognition when myosin IIB molecules assemble into homo-filament.
Type: article
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 高橋 正行

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