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Biochem Biophys Res Commun. 2003 Jan 17;300(3):679-85.

Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo.

Author information

1
National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.

Abstract

The 14-3-3 protein family associates with many proteins involved in intracellular signalling. In many cases, there is a distinct preference for a particular isoform(s) of 14-3-3. A specific repertoire of 14-3-3 dimer formation may therefore influence which of the interacting proteins could be brought together. We have analysed the pattern of dimer formation for two of the most abundant isoforms of 14-3-3, epsilon ( epsilon ) and gamma (gamma), following their stable expression. This revealed a distinct preference for particular dimer combinations that is largely independent of cellular conditions. gamma 14-3-3 occurred as homodimers and also formed heterodimers, mainly with epsilon 14-3-3 (In PC12 and Cos cells). The epsilon isoform formed heterodimers with 14-3-3 beta, gamma, zeta, and eta, but no homodimers were detected. The two 14-3-3 homologues, BMH1 and BMH2 from Saccharomyces cerevisiae, were mainly heterodimers.

PMID:
12507503
DOI:
10.1016/s0006-291x(02)02902-9
[Indexed for MEDLINE]

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