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Vol. 10, Issue 7, 2265-2283, July 1999
Department of Molecular and Cell Biology, University of California,
Berkeley, California 94720-3202
Sla2p, also known as End4p and Mop2p, is the founding member of a
widely conserved family of actin-binding proteins, a distinguishing feature of which is a C-terminal region homologous to the C
terminus of talin. These proteins may function in actin
cytoskeleton-mediated plasma membrane remodeling. A human homologue of
Sla2p binds to huntingtin, the protein whose mutation results in
Huntington's disease. Here we establish by immunolocalization that
Sla2p is a component of the yeast cortical actin cytoskeleton. Deletion analysis showed that Sla2p contains two separable regions, which can
mediate association with the cortical actin cytoskeleton, and which can
provide Sla2p function. One localization signal is actin based, whereas
the other signal is independent of filamentous actin. Biochemical
analysis showed that Sla2p exists as a dimer in vivo. Two-hybrid
analysis revealed two intramolecular interactions mediated by
coiled-coil domains. One of these interactions appears to underlie
dimer formation. The other appears to contribute to the regulation of
Sla2p distribution between the cytoplasm and plasma membrane. The data
presented are used to develop a model for Sla2p regulation and interactions.
Corresponding author. E-mail address:
drubin{at}uclink4.berkeley.edu.
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