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Vol. 10, Issue 4, 1077-1092, April 1999
and
*Department of Biochemistry and Molecular Biology, Louisiana State
University Medical Center, Shreveport, Louisiana 71130; and
Casein kinase 1 protein kinases are ubiquitous and abundant
Ser/Thr-specific protein kinases with activity on acidic substrates. In
yeast, the products of the redundant YCK1 and
YCK2 genes are together essential for cell viability.
Mutants deficient for these proteins display defects in cellular
morphogenesis, cytokinesis, and endocytosis. Yck1p and Yck2p are
peripheral plasma membrane proteins, and we report here that the
localization of Yck2p within the membrane is dynamic through the cell
cycle. Using a functional green fluorescent protein (GFP) fusion, we
have observed that Yck2p is concentrated at sites of polarized growth
during bud morphogenesis. At cytokinesis, GFP-Yck2p becomes associated
with a ring at the bud neck and then appears as a patch of
fluorescence, apparently coincident with the dividing membranes. The
bud neck association of Yck2p at cytokinesis does not require an intact septin ring, and septin assembly is altered in a Yck-deficient mutant.
The sites of GFP-Yck2p concentration and the defects observed for
Yck-deficient cells together suggest that Yck plays distinct roles in
morphogenesis and cytokinesis that are effected by differential localization.
Department of Zoology, University of Texas, Austin,
Texas 78712
Corresponding author. E-mail address:
lrobin{at}lsumc.edu.
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