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Molecular biological approaches to study myosin functions in cytokinesis of Dictyostelium
Author(s) -
Uyeda Taro Q.P.,
Yumura Shigehiko
Publication year - 2000
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/(sici)1097-0029(20000415)49:2<136::aid-jemt5>3.0.co;2-f
Subject(s) - cytokinesis , myosin , dictyostelium , dictyostelium discoideum , cleavage furrow , biology , microbiology and biotechnology , actin , cytoskeleton , myosin light chain kinase , molecular motor , cell division , genetics , gene , cell
The cellular slime mold Dictyostelium discoideum is amenable to biochemical, cell biological, and molecular genetic analyses, and offers a unique opportunity for multifaceted approaches to dissect the mechanism of cytokinesis. One of the important questions that are currently under investigation using Dictyostelium is to understand how cleavage furrows or contractile rings are assembled in the equatorial region. Contractile rings consist of a number of components including parallel filaments of actin and myosin II. Phenotypic analyses and in vivo localization studies of cells expressing mutant myosin IIs have demonstrated that myosin II's transport to and localization at the equatorial region does not require regulation by phosphorylation of myosin II, specific amino acid sequences of myosin II, or the motor activity of myosin II. Rather, the transport appears to depend on a myosin II‐independent flow of cortical cytoskeleton. What drives the flow of cortical cytoskeleton is still elusive. However, a growing number of mutants that affect assembly of contractile rings have been accumulated. Analyses of these mutations, identification of more cytokinesis‐specific genes, and information deriving from other experimental systems, should allow us to understand the mechanism of contractile ring formation and other aspects of cytokinesis. Microsc. Res. Tech. 49:136–144, 2000. © 2000 Wiley‐Liss, Inc.