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PMID: 10431818 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4.

FEBS letters ·Vol. 454 ·No. 3 ·1999-07-09 ·Pages 257-61

Martinez-Noel G, Niedenthal R, Tamura T, Harbers K

Abstract

The ubiquitin-conjugating enzyme UbcM4 was previously shown to be necessary for normal mouse development. As a first step in identifying target proteins or proteins involved in the specificity of UbcM4-mediated ubiquitylation, we have isolated seven cDNAs encoding proteins that specifically interact with UbcM4 but with none of the other Ubcs tested. This interaction was observed in yeast as well as in mammalian cells. With one exception, all UbcM4-interacting proteins (UIPs) belong to a family of proteins that contain a RING finger motif. As they are structurally related to RING finger proteins that have recently been shown to play an essential role in protein ubiquitylation and degradation, the possibility is discussed that UIPs are involved in the specific recognition of substrate proteins of UbcM4.

MeSH Terms
Amino Acid Sequence Animals DNA-Binding Proteins/metabolism Ligases/metabolism Mice Molecular Sequence Data Protein Binding Saccharomyces cerevisiae Sequence Alignment Substrate Specificity Ubiquitin-Conjugating Enzymes Zinc Fingers
Chemicals
DNA-Binding Proteins Ube2l3 protein, mouse Ubiquitin-Conjugating Enzymes Ligases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Martinez-Noel G
Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, Germany.
Niedenthal R
Tamura T
Harbers K
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1999-07-09
Pages
257-61
Language
English
Region
England
NLM ID
0155157
Subset
IM
Databases
GENBANK
AF124663, AF124664
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