ArticleJournal of protein chemistry1997
Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways.
Article in Journal of protein chemistry, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Pathways to Parkinson's disease: a spotlight on 14-3-3 proteins.NPJ Parkinson's disease · 2021Review
- Phosphoproteomics analysis of male and female Schistosoma mekongi adult worms.Scientific reports · 2019Article
- Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle.Redox biology · 2018Article
- IL-4 enhances survival of in vitro-differentiated mouse basophils through transcription-independent signaling downstream of PI3K.Cell death & disease · 2018Article
- Proteome and phosphoproteome characterization reveals new response and defense mechanisms of Brachypodium distachyon leaves under salt stress.Molecular & cellular proteomics : MCP · 2014Article
- Dual phosphorylation of Btk by Akt/protein kinase b provides docking for 14-3-3ζ, regulates shuttling, and attenuates both tonic and induced signaling in B cells.Molecular and cellular biology · 2013Article
- 14-3-3-regulated Ca(2+)-dependent protein kinase CPK3 is required for sphingolipid-induced cell death in Arabidopsis.Cell death and differentiation · 2013Article
- 14-3-3 phosphoprotein interaction networks - does isoform diversity present functional interaction specification?Frontiers in plant science · 2012Article
- Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.Molecular biology of the cell · 2003Article
- Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3.The Journal of physiology · 2002Article
- 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity.The EMBO journal · 2002Article
- 14-3-3 proteins; bringing new definitions to scaffolding.Oncogene · 2001Review
- 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation.The Biochemical journal · 2000Article
- alpha-Synuclein shares physical and functional homology with 14-3-3 proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 14-3-3 family are homo- and heterodimeric proteins whose biological role has been unclear for some time, although they are now gaining acceptance as a novel type of 'adaptor' protein that modulates interactions between components of signal transduction pathways, rather than by direct activation or inhibition. It is becoming apparent that phosphorylation of the binding partner and possibly also the 14-3-3 proteins may regulate these interactions. 14-3-3 isoforms interact with a novel phosphoserine (Sp) motif on many proteins, RSX1,2SpXP. The two isoforms that interact with Raf-1 are phosphorylated in vivo on Ser185 in a consensus sequence motif for proline-directed kinases. The crystal structure of 14-3-3 indicates that this phosphorylation could regulate interaction of 14-3-3 with its target proteins. We have now identified a number of additional phosphorylation sites on distinct mammalian and yeast isoforms.
Indexed as
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Registered trials
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