Li H, Pagé N, Bussey H
Yeast. 2002 Sep 30;19(13):1097–112
The cytoplasmic tail of Kre6p, a Golgi membrane protein involved in cell wall synthesis, interacts with the actin patch assembly components Las17pand Sla1p in a two-hybrid assay, and Kre6p co-immunoprecipitates with Las17p. Kre6p showed extensive co-localization with Och1p-containing cis-Golgi vesicles. The correct localization of Kre6p requires its cytoplasmic tail, Las17p, Sla1p and Vrp1p, suggesting that the cytoplasmic tail of Kre6pacts as a receptor, linking this cis-Golgi protein to Las17p and Sla1p. The actin patch assembly mutants las17 delta, sla1delta and vrp1 delta showed elevated levels of cell wall beta-1,6-glucan, and mutant cells were capable of only a limited number of cell divisions compared to wild-type. EM image analysis and beta-1,6-glucan localization indicated abnormal wall proliferation in the mother cells of these mutants. The pattern of cell wallhypertrophy indicates a failure to restrict cell wall growth to the bud.