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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

Lorick, Kevin L., Jensen, Jane P., Fang, Shengyun, Ong, Albert M., Hatakeyama, Shigetsugu, Weissman, Allan M.·1999·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.96.20.11364
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Abstract

A RING finger-containing protein (AO7) that binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination was identified. Mutations of cation-coordinating residues within AO7’s RING finger abolished ubiquitination, as did chelation of zinc. Several otherwise-unrelated RING finger proteins, including BRCA1, Siah-1, TRC8, NF-X1, kf-1, and Praja1, were assessed for their ability to facilitate E2-dependent ubiquitination. In all cases, ubiquitination was observed. The RING fingers were implicated directly in this activity through mutations of metal-coordinating residues or chelation of zinc. These findings suggest that a large number of RING finger-containing proteins, with otherwise diverse structures and functions, may play previously unappreciated roles in modulating protein levels via ubiquitination.

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Metadata

Authors
Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M.
Affiliations
Laboratory of Immune Cell Biology, Division of Basic Sciences, National Cancer Institute, Building 10, Room 1B34, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892-1152
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1999-09-28
Volume
96
Issue
20
Pages
11364-11369
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.96.20.11364
Cited by
981
References
1
Language
en

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