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*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

142 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
Externally publishedYes

Keywords

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

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