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Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis ‐Golgi protein Kre6p
Author(s) -
Li Huijuan,
Pagé Nicolas,
Bussey Howard
Publication year - 2002
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.904
Subject(s) - biology , golgi apparatus , microbiology and biotechnology , cytoplasm , mutant , actin , subcellular localization , biochemistry , gene , endoplasmic reticulum
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.