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

Ido Amit, 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

Research output: Contribution to journalArticlepeer-review

138 Scopus citations

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.

Original languageEnglish
Pages (from-to)1737-1752
Number of pages16
JournalGenes and Development
Volume18
Issue number14
DOIs
StatePublished - 15 Jul 2004

Keywords

  • Endocytosis
  • Growth factor
  • HIV
  • Signal transduction
  • Ubiquitin

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