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|Title:||The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast||Authors:||Naqvi, S.N.
|Issue Date:||27-Aug-1998||Citation:||Naqvi, S.N., Zahn, R., Mitchell, D.A., Stevenson, B.J., Munn, A.L. (1998-08-27). The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Current Biology 8 (17) : 959-962. ScholarBank@NUS Repository.||Abstract:||Several end mutations that block the internalisation step of endocytosis in Saccharomyces cerevisiae also affect the cortical actin cytoskeleton. END5 encodes a proline-rich protein (End5p or verprolin) required for a polarised cortical actin cytoskeleton and endocytosis. End5p interacts with actin, but its exact function is not yet known. To help elucidate End5p function, we sought other End5p-interacting proteins and identified the LAS17/BEE1 gene (encoding the yeast homologue of the human Wiskott-Aldrich Syndrome protein, WASp) as a high-copy-number suppressor of the temperature-sensitive growth and endocytic defects of end5-1 cells (carrying a frameshift mutation affecting the last 213 residues of End5p). LAS17 is unable to suppress a full deletion of END5 (end5Δ), however, suggesting that the defective End51p in end5-1 mutants may be stabilised by Las17p. The amino terminus of Las17p interacts with the carboxyl terminus of End5p in the yeast two-hybrid system and similar interactions have been shown between WASp and a mammalian End5p homologue, WASp-interacting protein (WIP). As las17Δ deletion mutants are blocked in endocytosis, we conclude that Las17p and End5p interact and are essential for endocytosis.||Source Title:||Current Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/134129||ISSN:||09609822|
|Appears in Collections:||Staff Publications|
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