Protection Against Osmotic Stress by cGMP-Mediated Myosin Phosphorylation
DISRUPTION
Threonine
Cytoplasm
HEAVY-CHAIN PHOSPHORYLATION
CYCLIC-AMP
SIGNAL-TRANSDUCTION
Myosins
03 medical and health sciences
Osmotic Pressure
Animals
Dictyostelium
Pseudopodia
Phosphorylation
Cyclic GMP
0303 health sciences
DICTYOSTELIUM-DISCOIDEUM
Water-Electrolyte Balance
GENE
Actins
REPLACEMENT
Actin Cytoskeleton
Glucose
MUTANTS
Guanylate Cyclase
LACKING
ATPASE ACTIVITY
DOI:
10.1126/science.271.5246.207
Publication Date:
2006-10-27T18:30:41Z
AUTHORS (4)
ABSTRACT
Conventional myosin functions universally as a generator of motive force in eukaryotic cells. Analysis of mutants of the microorganism
Dictyostelium discoideum
revealed that myosin also provides resistance against high external osmolarities. An osmo-induced increase of intracellular guanosine 3′,5′-monophosphate was shown to mediate phosphorylation of three threonine residues on the myosin tail, which caused a relocalization of myosin required to resist osmotic stress. This redistribution of myosin allowed cells to adopt a spherical shape and may provide physical strength to withstand extensive cell shrinkage in high osmolarities.
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