Reference: Li H, et al. (2002) Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p. Yeast 19(13):1097-112

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Abstract


The cytoplasmic tail of Kre6p, a Golgi membrane protein involved in cell wall synthesis, interacts with the actin patch assembly components Las17p and 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 Kre6p acts 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 wall hypertrophy indicates a failure to restrict cell wall growth to the bud.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Li H, Pagé N, Bussey H
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