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Vol. 9, Issue 1, 75-88, January 1998
Department of Cell Biology, Duke University Medical Center, Durham,
North Carolina 27710
The class I myosins play important roles in controlling many
different types of actin-based cell movements.
Dictyostelium cells either lacking or overexpressing
amoeboid myosin Is have significant defects in cortical activities such
as pseudopod extension, cell migration, and macropinocytosis. The
existence of Dictyostelium null mutants with strong
phenotypic defects permits complementation analysis as a means of
exploring important functional features of the myosin I heavy chain.
Mutant Dictyostelium cells lacking two myosin Is exhibit
profound defects in growth, endocytosis, and rearrangement of F-actin.
Expression of the full-length myoB heavy chain in these cells fully
rescues the double mutant defects. However, mutant forms of the myoB
heavy chain in which a serine at the consensus phosphorylation site has
been altered to an alanine or in which the C-terminal SH3 domain has
been removed fail to complement the null phenotype. The wild-type and
mutant forms of the myoB heavy chain appeared to be properly localized
when they were expressed in the myosin I null mutants. These results suggest that the amoeboid myosin I consensus phosphorylation site and
SH3 domains do not play a role in the localization of myosin I, but are
absolutely required for in vivo function.
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