Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis (Q24291878)

Experimental Cell Research

GOA release 2020-03-11

1

R R Subramanian

R R

Subramanian

1 reference

30 October 2023

S C Masters

2

S C

Masters

1 reference

30 October 2023

H Zhang

series ordinal

3

author given names

H

author last names

Zhang

1 reference

30 October 2023

H Fu

series ordinal

4

author given names

H

author last names

Fu

1 reference

30 October 2023

language of work or name

English

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publication date

15 November 2001

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published in

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volume

271

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issue

1

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page(s)

142-51

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cites work

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14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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The structural basis for 14-3-3:phosphopeptide binding specificity

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Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta

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The complexity of Raf-1 regulation

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The protein kinase KSR interacts with 14-3-3 protein and Raf.

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14-3-3sigma is a p53-regulated inhibitor of G2/M progression

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Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

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Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A

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Activation of Raf-1 by 14-3-3 proteins

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Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

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Crystal structure of the zeta isoform of the 14-3-3 protein

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14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage

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High frequency of hypermethylation at the 14-3-3 sigma locus leads to gene silencing in breast cancer

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Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism

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Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases

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The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family

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14-3-3 proteins associate with cdc25 phosphatases

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Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells

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Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins

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Activation-modulated association of 14-3-3 proteins with Cbl in T cells

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14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules

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Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein

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Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motif

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Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.

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Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein

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14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction

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Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase.

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14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove

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14-3-3 proteins interact with specific MEK kinases

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p90(RSK) blocks bad-mediated cell death via a protein kinase C-dependent pathway

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Cloning and characterization of the epsilon and zeta isoforms of the 14-3-3 proteins

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14-3-3 inhibits Bad-induced cell death through interaction with serine-136

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Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216

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Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt

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Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD

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Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms

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Interaction of the protein kinase Raf-1 with 14-3-3 proteins

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7 January 2021

Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation

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7 January 2021

Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase

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7 January 2021

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

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7 January 2021

p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis

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https://api.crossref.org/works/10.1006%2FEXCR.2001.5376

7 January 2021

14-3-3 proteins: structure, function, and regulation

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https://api.crossref.org/works/10.1006%2FEXCR.2001.5376

7 January 2021

Fundamental principles of in situ hybridization

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7 January 2021