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J. Cell Biol.,
Volume 143, Number 3, November 2, 1998 719-736
Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599
To identify septin-interacting proteins in
Saccharomyces cerevisiae, we screened for mutations
that are synthetically lethal with a cdc12 septin mutation. One of the genes identified was GIN4, which encodes a protein kinase related to Hsl1p/Nik1p and Ycl024Wp in S. cerevisiae and to Nim1p/Cdr1p and
Cdr2p in Schizosaccharomyces pombe. The Gin4p kinase domain displayed a two-hybrid interaction with
the COOH-terminal portion of the Cdc3p septin, and
Gin4p colocalized with the septins at the mother-bud
neck. This localization depended on the septins and on
the COOH-terminal (nonkinase) region of Gin4p, and
overproduction of this COOH-terminal region led to a
loss of septin organization and associated morphogenetic defects. We detected no effect of deleting
YCL024W, either alone or in combination with deletion of GIN4. Deletion of GIN4 was not lethal but led
to a striking reorganization of the septins accompanied
by morphogenetic abnormalities and a defect in cell separation; however, remarkably, cytokinesis appeared
to occur efficiently. Two other proteins that localize to
the neck in a septin-dependent manner showed similar
reorganizations and also appeared to remain largely
functional. The septin organization observed in gin4
vegetative cells resembles that seen normally in cells responding to mating pheromone, and no Gin4p was detected in association with the septins in such cells. The
organization of the septins observed in gin4 cells and
in cells responding to pheromone appears to support
some aspects of the model for septin organization suggested previously by Field et al. (Field, C.M., O. Al-Awar, J. Rosenblatt, M.L. Wong, B. Alberts, and T.J. Mitchison. 1996. J. Cell Biol. 133:605-616).
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