Literature DB >> 7615088

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

D H Jones1, S Ley, A Aitken.   

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.

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Year:  1995        PMID: 7615088     DOI: 10.1016/0014-5793(95)00598-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  75 in total

Review 1.  14-3-3 proteins: eukaryotic regulatory proteins with many functions.

Authors:  C Finnie; J Borch; D B Collinge
Journal:  Plant Mol Biol       Date:  1999-07       Impact factor: 4.076

Review 2.  Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.

Authors:  Alastair Aitken
Journal:  Plant Mol Biol       Date:  2002-12       Impact factor: 4.076

3.  Expression profiling of the 14-3-3 gene family in response to salt stress and potassium and iron deficiencies in young tomato (Solanum lycopersicum) roots: analysis by real-time RT-PCR.

Authors:  Wei Feng Xu; Wei Ming Shi
Journal:  Ann Bot       Date:  2006-08-30       Impact factor: 4.357

4.  Structural basis for protein-protein interactions in the 14-3-3 protein family.

Authors:  Xiaowen Yang; Wen Hwa Lee; Frank Sobott; Evangelos Papagrigoriou; Carol V Robinson; J Günter Grossmann; Michael Sundström; Declan A Doyle; Jonathan M Elkins
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-03       Impact factor: 11.205

5.  DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.

Authors:  Mónica Alvarez; Xavier Altafaj; Sergi Aranda; Susana de la Luna
Journal:  Mol Biol Cell       Date:  2007-01-17       Impact factor: 4.138

Review 6.  14-3-3 proteins in platelet biology and glycoprotein Ib-IX signaling.

Authors:  Yunfeng Chen; Zaverio M Ruggeri; Xiaoping Du
Journal:  Blood       Date:  2018-04-05       Impact factor: 22.113

7.  14-3-3 proteins are required for maintenance of Raf-1 phosphorylation and kinase activity.

Authors:  J A Thorson; L W Yu; A L Hsu; N Y Shih; P R Graves; J W Tanner; P M Allen; H Piwnica-Worms; A S Shaw
Journal:  Mol Cell Biol       Date:  1998-09       Impact factor: 4.272

8.  14-3-3 sigma positively regulates p53 and suppresses tumor growth.

Authors:  Heng-Yin Yang; Yu-Ye Wen; Chih-Hsin Chen; Guillermina Lozano; Mong-Hong Lee
Journal:  Mol Cell Biol       Date:  2003-10       Impact factor: 4.272

9.  Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo.

Authors:  N Philip; S F Acevedo; E M Skoulakis
Journal:  J Neurosci       Date:  2001-11-01       Impact factor: 6.167

10.  Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function.

Authors:  N Meller; Y C Liu; T L Collins; N Bonnefoy-Bérard; G Baier; N Isakov; A Altman
Journal:  Mol Cell Biol       Date:  1996-10       Impact factor: 4.272

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