14-3-3 proteins: biological function and domain structure

Aitken, Alastair; Jones, David H.; Soneji, Yasmina; Howell, Steve

doi:10.1042/bst0230605

Cited by 126 publications

(101 citation statements)

References 9 publications

(15 reference statements)

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“…The 14-3-3 family of proteins are highly conserved proteins ubiquitously expressed in all eukaryotic cells (Aitken et al, 1995). Members of the 14-3-3 family proteins have been shown to interact with many key signaling molecules to regulate intracellular signaling events in cell proliferation, di erentiation and apoptosis (Bonnefoy-Berard et al, 1995;Craparo et al, 1997;Fu et al, 1994;Garcia-Guzman et al, 1999;Hausser et al, 1999;Liu et al, 1997;Meller et al, 1996;Reuther et al, 1994;Zhang et al, 1997.…”

Section: Discussionmentioning

confidence: 99%

“…14-3-3 proteins have been shown to bind speci®c phosphoserine-containing motifs, RSXpSXP and RXY/FXpSXP present in many of its binding partners (Aitken et al, 1995;Muslin et al, 1996; Ya e et al, 1997). Although it was reported to be phosphorylated under some conditions (Hynes, 1992), the single serine residue in the cytoplasmic domain of integrin b1 is not present in these motifs.…”

Section: Discussionmentioning

confidence: 99%

“…14-3-3 proteins are a highly conserved family of dimeric proteins ubiquitously expressed in all eukaryotic cells (for review, see Fu et al, 2000;Aitken et al, 1995). Members of 14-3-3 family proteins have been shown to bind a number of signaling molecules by both phosphoserine motifs (Muslin et al, 1996;Ya e et al, 1997) and non-phosphoserine mechanism (Clark et al, 1997;Masters et al, 1999;Wang et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Identification of a novel interaction between integrin β1 and 14-3-3β

2001

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of a novel interaction between integrin β1 and 14-3-3β

2001

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“…It also has been associated with synaptic structures and has been implicated in the regulation of exocytosis. Its biochemical properties and physiological interactions are summarized in a number of reviews (32,33).…”

mentioning

confidence: 99%

Rethinking the role of phosducin: Light-regulated binding of phosducin to 14-3-3 in rod inner segments

Nakano

Chen

Tarr

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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Phosducin (Pd), a small protein found abundantly in photoreceptors, is widely assumed to regulate light sensitivity in the rod outer segment through interaction with the heterotrimeric G protein transducin. But, based on histochemistry and Western blot analysis, Pd is found almost entirely in the inner segment in both light and dark, most abundantly near the rod synapse. We report a second small protein, 14-3-3, in the rod with a similar distribution. By immunoprecipitation, phospho-Pd is found to interact with 14-3-3 in material from dark-adapted retina, and this interaction is markedly diminished by light, which dephosphorylates Pd. Conversely, unphosphorylated Pd binds to inner segment G protein(s) in the light. From these results and reported functions of 14-3-3, we have constructed a hypothesis for the regulation of light sensitivity at the level of rod synapse. By dissociating the Pd͞14-3-3 complex, light enables both proteins to function in this role.

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“…However, the exact role of 3BP2 in hematopoietic/lymphoid cell signaling remains ill-defined. The 14-3-3 protein family constitutes a highly conserved group family of molecules present in high abundance in all eukaryotic cells (15,16). They mediate signal transduction, cell cycle control, apoptosis, stress response, and malignant transformation by binding to phosphoserine-containing proteins such as c-Raf, Cdc25c, and BAD (17).…”

mentioning

confidence: 99%

The Chaperone Protein 14-3-3 Interacts with 3BP2/SH3BP2 and Regulates Its Adapter Function

Foucault¹,

Liu²,

Bernard³

et al. 2003

Journal of Biological Chemistry

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Lymphocyte stimulation by immunoreceptors is achieved through the activation of multiple signaling pathways leading to cytokine gene transcription. Adapter proteins are critical signaling components that can integrate multiple pathways by allowing the assembly of multimolecular signaling complexes. We previously showed that the cytoplasmic adapter 3BP2 (also known as SH3BP2) promotes NFAT/AP-1 transcriptional activities in T cells through the activation of Ras-and calcineurin-dependent pathways. However, the molecular mechanisms by which 3BP2/SH3BP2 regulates cell signaling and activation remain poorly documented. In this study, using a combination of yeast two-hybrid analysis and biochemical approaches, we present evidence for a physical interaction between 3BP2 and the chaperone protein 14-3-3. This interaction was direct and constitutively detected in yeast and in mammalian cells. Phorbol ester, pervanadate, and forskolin/isobutylmethylxanthine stimulations enhanced this interaction, as well as co-expression of constitutive active mutants of serine/threonine kinases, including protein kinase C. We found that dephosphorylation of 3BP2 by alkaline phosphatase disrupted its interaction with 14-3-3 and that 3BP2 was a substrate of purified protein kinase C in vitro, suggesting that the phosphorylation of 3BP2 by upstream kinases was required for 14-3-3 binding. Using deletion mutants of 3BP2, two 14-3-3 binding domains were mapped to two proline-rich (residues 201-240 and 270 -310) domains of 3BP2. These domains were shown to contain two 14-3-3 consensus binding motifs. We identified residues Ser 225 and Ser 277 of 3BP2 as being essential for interaction with 14-3-3 family proteins, optimal 3BP2 serine phosphorylation, and then for 3BP2-dependent function. Indeed, a 3BP2 mutant protein incapable of binding 14-3-3 showed increased capacity to stimulate NFAT transcriptional activities, suggesting that 14-3-3 binding to 3BP2 negatively regulates 3BP2 adapter function in lymphocytes.

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14-3-3 proteins: biological function and domain structure

Cited by 126 publications

References 9 publications

Identification of a novel interaction between integrin β1 and 14-3-3β

Identification of a novel interaction between integrin β1 and 14-3-3β

Rethinking the role of phosducin: Light-regulated binding of phosducin to 14-3-3 in rod inner segments

The Chaperone Protein 14-3-3 Interacts with 3BP2/SH3BP2 and Regulates Its Adapter Function

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