4.5 Article

E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme

Journal

FEBS LETTERS
Volume 503, Issue 1, Pages 61-64

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(01)02689-8

Keywords

Huntingtin-interacting protein-2; RING motif; ubiquitin-conjugating enzyme; ubiquitin ligase; yeast two-hybrid

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To identify proteins that interact with Huntingtin-interacting protein-2 (Hip-2), a ubiquitin-conjugating enzyme, a yeast two-hybrid screen system was used to isolate five positive clones. Sequence analyses showed that, with one exception, all Hip-2-interacting proteins Contained the RING finger motifs. The interaction of Hip-2 with RNF2, one of the clones, was further confirmed through in vitro and in vivo experiments. Mutations in the RING domain of RNF2 prevented the clone from binding to Hip-2, an indication that the RING domain is the binding determinant. RNF2 showed a ubiquitin ligase (E3) activity in the presence of Hip-2, suggesting that a subset of RING finger proteins may have roles as Us. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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