Phospholipase C interacts with @entity70927 and is required for expression of XXXX and osmoresistance in @entity375 .

@entity1 @entity10612 @entity27032 @entity653 @entity18385 @entity57497 @entity7685 @entity375 @entity70927
The @entity375 @entity57497 gene encodes a homolog of the delta isoform of @entity1 phosphoinositide-specific phospholipase C. Cells deleted for @entity57497 ( @entity57497 ) are viable, but display several phenotypes, including osmotic, temperature, and @entity10612 sensitivity. We have used a two-hybrid screen to identify @entity57497 -interacting proteins. One of the interacting proteins found was @entity70927 , a recently identified, essential, nuclear protein. The @entity70927 gene was originally cloned by complementation of an osmostress-sensitive mutant. The @entity57497 - @entity70927 interaction was confirmed biochemically by affinity chromatography. @entity70927 interacts genetically with both @entity57497 and @entity18385 (which encodes an osmosensing mitogen-activated protein kinase). Overexpression of @entity70927 suppresses the temperature sensitivity of cells bearing the @entity57497 -4 allele, and the double mutant strain @entity57497 Delta @entity70927 -1 displays enhanced temperature and @entity10612 sensitivity. The @entity57497 hog1Delta strain displays increased osmosensitivity, and has a synthetic defect in @entity653 synthesis and the expression of @entity27032 (which encodes the enzyme @entity7685 dehydrogenase that is involved in @entity653 biosynthesis), suggesting that @entity57497 and @entity18385 function in independent pathways. The @entity18385 Delta @entity70927 -1 double mutant displays enhanced osmosensitivity relative to that of either single mutant. The triple mutant @entity57497 hog1Delta @entity70927 -1 is inviable, while the @entity57497 hog1Delta @entity70927 -2 strain grows extremely slowly and is more osmosensitive than the @entity57497 hog1Delta or @entity18385 Delta @entity70927 -2 strain. These results are consistent with a model in which @entity57497 and @entity18385 function in parallel pathways affecting osmoregulation, and signals from both these pathways converge, at least partly, on @entity70927 .
