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PMID: 7615088 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins.

FEBS letters ·Vol. 368 ·No. 1 ·1995-07-10 ·Pages 55-8

Jones DH, Ley S, Aitken A

Abstract

14-3-3 proteins play a role in many cellular functions: they bind to and regulate several proteins which are critical for cell proliferation and differentiation. 14-3-3 proteins exist as dimers, and in this study we have shown that diverse 14-3-3 proteins can form both homo- and heterodimers in vitro (by cross-linking studies) and in vivo (by coimmunoprecipitation and Western blot analysis); this interaction is mediated solely through the N-terminal domain of the proteins. The composition of 14-3-3 dimers within a cell may play a key part in the role of this family of proteins as modulators or adapters which facilitate the interaction of distinct components of signalling pathways.

MeSH Terms
14-3-3 Proteins Base Sequence Cell Line Cloning, Molecular Cross-Linking Reagents Escherichia coli Humans Molecular Sequence Data Proteins/chemistry,physiology Signal Transduction/physiology Structure-Activity Relationship Tyrosine 3-Monooxygenase
Chemicals
14-3-3 Proteins Cross-Linking Reagents Proteins Tyrosine 3-Monooxygenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jones D H
Division of Protein Structure, National Institute for Medical Research, London, UK.
Ley S
Aitken A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-07-10
Pages
55-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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