Myosin II heavy chain null mutant of Dictyostelium exhibits defective intracellular particle movement.
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چکیده
منابع مشابه
Myosin II heavy chain null mutant of Dictyostelium exhibits defective intracellular particle movement
Both cellular motility and intracellular particle movement are compared between normal Dictyostelium amebae of strain AX4 and amebae of a myosin II heavy chain null mutant, HS2215, using the computer assisted "Dynamic Morphology System." In AX4 cells rapidly translocating in buffer, cytoplasmic expansion is apical and the majority of intracellular particles move anteriorly, towards the site of ...
متن کاملDictyostelium myosin II null mutant can still cap Con A receptors.
Cross-linked antigens on the surface of a motile cell cap at the trailing end of the cell. In Dictyostelium discoideum, myosin II null mutants have previously been reported to be unable to cap Con A receptors, although they are able to locomote. This finding implicated myosin II as an essential component of the capping mechanism, although not of the machinery for locomotion. Here we show that m...
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How myosin II localizes to the cleavage furrow of dividing cells is largely unknown. We show here that a 283-residue protein, assembly domain (AD)1, corresponding to the AD in the tail of Dictyostelium myosin II assembles into bundles of long tubules when expressed in myosin II-null cells and localizes to the cleavage furrow of dividing cells. AD1 mutants that do not polymerize in vitro do not ...
متن کاملSpecific phosphorylation of threonine by the Dictyostelium myosin II heavy chain kinase family.
Dictyostelium myosin II heavy chain kinase A (MHCK A), MHCK B, and MHCK C contain a novel type of protein kinase catalytic domain that displays no sequence identity to the catalytic domain present in conventional serine, threonine, and/or tyrosine protein kinases. Several proteins, including myelin basic protein, myosin regulatory light chain, caldesmon, and casein were phosphorylated by the ba...
متن کاملMultiple myosin II heavy chain kinases: roles in filament assembly control and proper cytokinesis in Dictyostelium.
Myosin II filament assembly in Dictyostelium discoideum is regulated via phosphorylation of residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail. A series of novel protein kinases in this system are capable of phosphorylating these residues in vitro, driving filament disassembly. Previous studies have demonstrated that at least three of these kinases (MHCK A...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1990
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.111.3.1137