Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis‐Golgi protein Kre6p

• Published in: Yeast (Chichester, England) Vol. 19; no. 13; pp. 1097 - 1112
• Main Authors: Li, Huijuan, Pagé, Nicolas, Bussey, Howard
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 30.09.2002
• Subjects: Actins - chemistry; Carrier Proteins - chemistry; Cell Wall - metabolism; cell wall synthesis; cortical actin patch assembly; Cytoplasm - chemistry; Cytoskeletal Proteins; Fungal Proteins - analysis; Fungal Proteins - chemistry; Golgi Apparatus - chemistry; Golgi vesicle receptor; Membrane Proteins - analysis; Membrane Proteins - chemistry; mother–daughter asymmetry; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins; Two-Hybrid System Techniques; Wiskott-Aldrich Syndrome Protein; β‐1,6‐glucan localization
• ISSN: 0749-503X; 1097-0061
• DOI: 10.1002/yea.904

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 las17Δ, sla1Δ and vrp1Δ showed elevated levels of cell wall β‐1,6‐glucan, and mutant cells were capable of only a limited number of cell divisions compared to wild‐type. EM image analysis and β‐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. Copyright © 2002 John Wiley & Sons, Ltd.