Activation of the 43 kDa Inositol Polyphosphate 5-Phosphatase by 14-3-3ζ

Campbell, Janine; Gurung, Rajendra; Romero, Susana; Speed, Caroline J.; Andrews, Robert K.; Berndt, Michael C.; Mitchell, Christina A.

doi:10.1021/bi9708085

Cited by 45 publications

(35 citation statements)

References 46 publications

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“…It is not uncommon to find examples in which dimerization of 14-3-3 is not essential for its function (25,26). Our studies provide evidence that binding of monomeric D14-3-3 is sufficient to change dSlo channel properties.…”

Section: Discussionmentioning

confidence: 61%

Monomeric 14-3-3 Protein Is Sufficient to Modulate the Activity of the Drosophila Slowpoke Calcium-dependent Potassium Channel

Zhou¹,

Reddy²,

Murrey

et al. 2003

Journal of Biological Chemistry

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Drosophila 14-3-3 (D14-3-3) modulates the activity of the Slowpoke calcium-dependent potassium channel (dSlo) by interacting with the dSlo binding protein, Slob. We show here that D14-3-3 forms dimers in vitro. Site-directed mutations in its putative dimerization interface result in a dimerization-deficient form of D14-3-3. Both the wild-type and dimerization-deficient forms of D14-3-3 bind to Slob with similar affinity and form complexes with dSlo. When dSlo and Slob are expressed in mammalian cells, the dSlo channel activity is similarly modulated by co-expression of either the wild-type or the dimerization-deficient form of D14-3-3. In addition, dSlo is still modulated by wild-type D14-3-3 in the presence of a 14-3-3 mutant, which does not itself bind to Slob but forms heterodimers with the wild-type 14-3-3. These data, taken together, suggest that monomeric D14-3-3 is capable of modulating dSlo channel activity in this regulatory complex.

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Section: Discussionmentioning

confidence: 61%

Monomeric 14-3-3 Protein Is Sufficient to Modulate the Activity of the Drosophila Slowpoke Calcium-dependent Potassium Channel

Zhou¹,

Reddy²,

Murrey

et al. 2003

Journal of Biological Chemistry

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“…However, 14-3-3 protein binding of nonphosphorylated targets has been reported previously (Masters et al, 1999), and can occur on nonphosphorylated RSXS consensus binding motifs (Campbell et al, 1997).…”

Section: Adam22 Cytoplasmic Domain Interacts With 14-3-3 Family Membersmentioning

confidence: 92%

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Gödde

D'Abaco

Paradiso

et al. 2006

Journal of Cell Science

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ADAM22 is one of three catalytically inactive ADAM family members highly expressed in the brain. ADAM22 has numerous splice variants, all with considerable cytoplasmic tails of up to 148 amino acids. ADAM22 can act to inhibit cell proliferation, however, it has been suggested that it also acts as an adhesion protein. We identified three 14-3-3 protein members by a yeast twohybrid screen and show by co-immunoprecipitation that the cytoplasmic domain of ADAM22 can interact with all six 14-3-3 proteins expressed in the brain. In addition, we show that 14-3-3 proteins interact preferentially with the serine phosphorylated precursor form of ADAM22. ADAM22 has two 14-3-3 protein binding consensus motifs; the first binding site, spanning residues 831-834, was shown to be the most crucial for 14-3-3 binding to occur. The interaction between ADAM22 and 14-3-3 proteins is dependent on phosphorylation of ADAM22, but not of 14-3-3 proteins. ADAM22 point mutants lacking functional 14-3-3 protein binding motifs could no longer accumulate efficiently at the cell surface. Deletion of both 14-3-3 binding sites and newly identified ER retention motifs restored localization of ADAM22 at the cell surface. These results reveal a role for 14-3-3 proteins in targeting ADAM22 to the membrane by masking ER retention signals.

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“…However, several reports have established that 14-3-3 proteins are also able to interact with non-phosphorylated ligands with high affinity (42)(43)(44)(45)(46)(47)(48). Clearly then, additional regulatory mechanisms must exist to ensure control of 14-3-3 biological function(s).…”

Section: -3-3 Expression and Phosphorylation During Cell Cycle Progmentioning

confidence: 99%

A Combined Proteome and Ultrastructural Localization Analysis of 14-3-3 Proteins in Transformed Human Amnion (AMA) Cells

Moreira

Shen

Ohlsson

et al. 2008

Molecular & Cellular Proteomics

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The 14-3-3 proteins constitute a family of highly conserved and broadly expressed multifunctional polypeptides that are involved in a variety of important cellular processes that include cell cycle progression, growth, differentiation, and apoptosis. Although the exact cellular function(s) of 14-3-3 proteins is not fully elucidated, as a rule these proteins act by binding to protein ligands, thus regulating their activity; so far more than 300 cellular proteins have been reported to interact with 14-3-3 proteins. Binding to cognate interacting partners is isoform-specific, but redundancy also exists as several binding peptides can be recognized by all isoforms, and some functions can be carried out by any isoform indistinctly. Moreover by interacting with different ligands in a spatially and temporally regulated fashion the same isoform can play multiple possibly even opposing roles where the resultant cellular outcome will be determined by the integration of the various effects. Although there is a large body of literature on specific aspects of 14-3-3 biology, not much is known on the coordinated aspects of 14-3-3 isoform expression, post-translational modifications, and subcellular localization. To address the question of isoform-specific differences, we carried out a comparative analysis of the patterns of expression, phosphorylation, and subcellular localization of the 14-3-3 ␤, , , , and protein isoforms in transformed human amnion (AMA) cells. To validate as well as broaden our observations we analyzed the occurrence of the various isoforms in a large number of established cell lines and mammary and urothelial tissue specimens. Given the systematic approach we undertook and our application of isoform-discriminating technologies to the analysis of various cellular systems, we expect the data presented in this study to serve as an enabling resource for researchers working with 14-3-3

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Activation of the 43 kDa Inositol Polyphosphate 5-Phosphatase by 14-3-3ζ

Cited by 45 publications

References 46 publications

Monomeric 14-3-3 Protein Is Sufficient to Modulate the Activity of the Drosophila Slowpoke Calcium-dependent Potassium Channel

Monomeric 14-3-3 Protein Is Sufficient to Modulate the Activity of the Drosophila Slowpoke Calcium-dependent Potassium Channel

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

A Combined Proteome and Ultrastructural Localization Analysis of 14-3-3 Proteins in Transformed Human Amnion (AMA) Cells

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