1. Academic Validation
  2. Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding

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

  • Genes Dev. 2004 Jul 15;18(14):1737-52. doi: 10.1101/gad.294904.
Ido Amit 1 Liat Yakir Menachem Katz Yaara Zwang Mina D Marmor Ami Citri Keren Shtiegman Iris Alroy Shmuel Tuvia Yuval Reiss Eli Roubini Maya Cohen Ron Wides Eran Bacharach Ullrich Schubert Yosef Yarden
Affiliations

Affiliation

  • 1 Department of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100, Israel.
Abstract

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.

Figures