The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast
The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast
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DOI：
10.1016/s0960-9822(98)70396-3
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发表时间：
1998-08-27
期刊：
影响因子：
9.2
通讯作者：
Munn, AL
中科院分区：
文献类型：
--
作者：
Naqvi, SN;Zahn, R;Munn, AL
阻断酿酒酵母内吞作用的内化步骤的几个末端突变也影响皮质肌动蛋白细胞骨架[1]，END 5编码极化皮质肌动蛋白细胞骨架和内吞作用所需的富含脯氨酸的蛋白（End 5 p或verprolin）[2，3]，End 5 p与肌动蛋白相互作用[4]，但其确切功能尚不清楚。为了帮助阐明End 5 p的功能，我们寻找了其他End 5 p相互作用蛋白，并鉴定了LAS 17/BEE 1基因（编码人Wiskott-Aldrich综合征蛋白WASp的酵母同源物）作为end 5 -1细胞的温度敏感性生长和内吞缺陷的高拷贝数抑制剂（携带影响End 5 p的最后213个残基的移码突变），LAS 17不能抑制END 5的完全缺失（end 5 Delta），然而，这表明在end 5 -1突变体中缺陷的End 5 - 1 p可以被Las 17 p稳定，Las 17 p的氨基末端与End 5 p的羧基末端在酵母双链中相互作用，在WASp和哺乳动物End 5 p同源物WASp-相互作用蛋白（WASp-interacting protein，WASP）之间已经显示了杂交系统和类似的相互作用[5]。由于Las 17 Delta缺失突变体在胞吞作用中被阻断，我们得出结论，Las 17 p和End 5 p相互作用并且对于胞吞作用是必需的。
Several end mutations that block the internalisation step of endocytosis in Saccharomyces cerevisiae also affect the cortical actin cytoskeleton [1], END5 encodes a proline-rich protein (End5p or verprolin) required for a polarised cortical actin cytoskeleton and endocytosis [2,3], End5p interacts with actin [4], 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 (end5 Delta), however, suggesting that the defective End5-1p 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) [5]. As las17 Delta deletion mutants are blocked in endocytosis, we conclude that Las17p and End5p interact and are essential for endocytosis.