The 14-3-3 proteins
نویسنده
چکیده
So what’s so interesting about them? In 1996 14-3-3 was found to bind to a variety of oncoproteins including Raf-1, polyoma middle T, and Bcr-Abl. Since then the 14-3-3 proteins have been shown to bind to a wide variety of proteins involved in signal transduction, cell cycle and apoptosis. These proteins include Cdc25, NFAT, Bad, Cbl, A20, PI 3-kinase, IRS-1, MEKK, p130Cas, glucocorticoid receptor and the forkhead transcription factor. So is there anything they don’t bind to? The list of proteins to which they bind grows every day. But we now know that 14-3-3 proteins bind to a specific serine phosphorylated sequence. Most of the known 14-3-3-binding proteins contain this motif.
منابع مشابه
Phosphorylation-Dependent Protein Interaction with Trypanosoma brucei 14-3-3 Proteins that Display Atypical Target Recognition
BACKGROUND The 14-3-3 proteins are structurally conserved throughout eukaryotes and participate in protein kinase signaling. All 14-3-3 proteins are known to bind to evolutionally conserved phosphoserine-containing motifs (modes 1 and/or 2) with high affinity. In Trypanosoma brucei, 14-3-3I and II play pivotal roles in motility, cytokinesis and the cell cycle. However, none of the T. brucei 14-...
متن کاملCell cycle roles for two 14-3-3 proteins during Drosophila development.
Drosophila 14-3-3 epsilon and 14-3-3 zeta proteins have been shown to function in RAS/MAP kinase pathways that influence the differentiation of the adult eye and the embryo. Because 14-3-3 proteins have a conserved involvement in cell cycle checkpoints in other systems, we asked (1) whether Drosophila 14-3-3 proteins also function in cell cycle regulation, and (2) whether cell proliferation dur...
متن کاملProteomic analysis of 14-3-3 zeta binding proteins in the mouse hippocampus.
14-3-3 proteins are ubiquitous molecular chaperones with important roles in brain development and neuronal function. Altered expression of 14-3-3 proteins has been reported in several neurologic and neurodegenerative disorders and identifying 14-3-3 binding proteins may provide important insights into the physiologic and pathophysiologic roles of these proteins. Particular interest has emerged ...
متن کاملMembrane proteins as 14-3-3 clients in functional regulation and intracellular transport.
14-3-3 proteins regulate the function and subcellular sorting of membrane proteins. Often, 14-3-3 binding to client proteins requires phosphorylation of the client, but the relevant kinase is unknown in most cases. We summarize current progress in identifying kinases that target membrane proteins with 14-3-3 binding sites and discuss the molecular mechanisms of 14-3-3 action. One of the kinases...
متن کاملSWTY--a general peptide probe for homogeneous solution binding assay of 14-3-3 proteins.
Dimeric 14-3-3 proteins exert diverse functions in eukaryotes by binding to specific phosphorylated sites on diverse target proteins. Critical to the physiological function of 14-3-3 proteins is the wide range of binding affinity to different ligands. The existing information of binding affinity is mainly derived from nonhomogeneous-based methods such as surface plasmon resonance and quantitati...
متن کاملInteraction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
The highly conserved and ubiquitously expressed 14-3-3 family of proteins bind to a variety of proteins involved in signal transduction and cell cycle regulation. The nature and specificity of 14-3-3 binding is, however, not known. Here we show that 14-3-3 is a specific phosphoserine-binding protein. Using a panel of phosphorylated peptides based on Raf-1, we have defined the 14-3-3 binding mot...
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ورودعنوان ژورنال:
- Current Biology
دوره 10 شماره
صفحات -
تاریخ انتشار 2000