Differential localization in cells of myosin II heavy chain kinases during cytokinesis and polarized migration.

ABSTRACT:

Background

Cortical myosin-II filaments in Dictyostelium discoideum display enrichment in the posterior of the cell during cell migration, and in the cleavage furrow during cytokinesis. Filament assembly in turn is regulated by phosphorylation in the tail region of the myosin heavy chain (MHC). Early studies have revealed one enzyme, MHCK-A, which participates in filament assembly control, and two other structurally related enzymes, MHCK-B and -C. In this report we evaluate the biochemical properties of MHCK-C, and using fluorescence microscopy in living cells we examine the localization of GFP-labeled MHCK-A, -B, and -C in relation to GFP-myosin-II localization.

Results

Biochemical analysis indicates that MHCK-C can phosphorylate MHC with concomitant disassembly of myosin I

SUBMITTER: Liang W 

PROVIDER: S-EPMC119860 | biostudies-literature | 2002 Jul

REPOSITORIES: biostudies-literature