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The Tail Domain of Myosin M Catalyses Nucleotide Exchange on Rac1 GTPases and Can Induce Actin‐Driven Surface Protrusions
Author(s) -
Geissler Heidrun,
Ullmann Ronald,
Soldati Thierry
Publication year - 2000
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2000.010505.x
Subject(s) - biology , guanine nucleotide exchange factor , rac1 , microbiology and biotechnology , myosin , gtpase , actin , nucleotide , rac gtp binding proteins , myosin light chain kinase , biophysics , biochemistry , signal transduction , gene
Members of the myosin superfamily play crucial roles in cellular processes including management of the cortical cytoskeleton, organelle transport and signal transduction. GTPases of the Rho family act as key control elements in the reorganization of the actin cytoskeleton in response to growth factors, and other functions such as membrane trafficking, transcriptional regulation, growth control and development. Here, we describe a novel unconventional myosin from Dictyostelium discoideum , MyoM. Primary sequence analysis revealed that it has the appearance of a natural chimera between a myosin motor domain and a guanine nucleotide exchange factor (GEF) domain for Rho GTPases. The functionality of both domains was established. Binding of the motor domain to F‐actin was ATP‐dependent and potentially regulated by phosphorylation. The GEF domain displayed selective activity on Rac1‐related GTPases. Overexpression, rather than absence of MyoM, affected the cell morphology and viability. Particularly in response to hypo‐osmotic stress, cells overexpressing the MyoM tail domain extended massive actin‐driven protrusions. The GEF was enriched at the tip of growing protuberances, probably through its pleckstrin homology domain. MyoM is the first unconventional myosin containing an active Rac‐GEF domain, suggesting a role at the interface of Rac‐mediated signal transduction and remodeling of the actin cytoskeleton.