Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding

被引:126
作者
Amit, I
Yakir, L
Katz, M
Zwang, Y
Marmor, MD
Citri, A
Shtiegman, K
Alroy, I
Tuvia, S
Reiss, Y
Roubini, E
Cohen, M
Wides, R
Bacharach, E
Schubert, U
Yarden, Y [1 ]
机构
[1] Weizmann Inst Sci, Dept Regulat Biol, IL-76100 Rehovot, Israel
[2] Proteologics Ltd, IL-76124 Rehovot, Israel
[3] Sigma Aldrich Israel Ltd, IL-76100 Rehovot, Israel
[4] Bar Ilan Univ, Dept Life Sci, IL-52900 Ramat Gan, Israel
[5] Tel Aviv Univ, Dept Cell Res & Immunol, IL-69978 Tel Aviv, Israel
[6] Univ Erlangen Nurnberg, Inst Clin & Mol Virol, D-91054 Erlangen, Germany
关键词
endocytosis; growth factor; HIV; ubiquitin; signal transduction;
D O I
10.1101/gad.294904
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The tumor suppressor gene 101 (tsg101) regulates vesicular trafficking processes in yeast and mammals. We report a novel protein, Tal (Tsg101-associated ligase), whose RING finger is necessary for multiple monoubiquitylation of Tsg101. Bivalent binding of Tsg101 to a tandem tetrapeptide motif (PTAP) and to a central region of Tal is essential for Tal-mediated ubiquitylation of Tsg101. By studying endocytosis of the epidermal growth factor receptor and egress of the human immunodeficiency virus, we conclude that Tal regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane.
引用
收藏
页码:1737 / 1752
页数:16
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