Oligomeric structure of 14-3-3 protein: what do we know about monomers? (Q38060462)

28 August 2017

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title

Oligomeric structure of 14-3-3 protein: what do we know about monomers? (English)

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28 August 2017

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Nikolai N Sluchanko

1

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28 August 2017

Nikolai B Gusev

series ordinal

2

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28 August 2017

language of work or name

English

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publication date

15 November 2012

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28 August 2017

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28 August 2017

volume

586

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28 August 2017

issue

24

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28 August 2017

page(s)

4249-4256

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Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.

28 August 2017

cites work

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21 January 2018

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14-3-3 proteins in neurodegeneration

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14-3-3 proteins as signaling integration points for cell cycle control and apoptosis

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14-3-3 proteins in cell cycle regulation

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14-3-3 proteins and regulation of cytoskeleton

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Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport

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14-3-3 proteins as potential therapeutic targets

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

21 January 2018

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

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins

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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

21 January 2018

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

21 January 2018

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Bioinformatic and experimental survey of 14-3-3-binding sites.

21 January 2018

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

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.

21 January 2018

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Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3gamma.

21 January 2018

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A novel function of 14-3-3 protein: 14-3-3zeta is a heat-shock-related molecular chaperone that dissolves thermal-aggregated proteins

21 January 2018

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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

21 January 2018

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14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232.

21 January 2018

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Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon

21 January 2018

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Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand binding

21 January 2018

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Cyclin D1 in low-dose radiation-induced adaptive resistance.

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Serine 58 of 14-3-3zeta is a molecular switch regulating ASK1 and oxidant stress-induced cell death

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3ζ homodimer interface

21 January 2018

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Characterization of 14-3-3sigma dimerization determinants: requirement of homodimerization for inhibition of cell proliferation

21 January 2018

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Structural basis for protein-protein interactions in the 14-3-3 protein family

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

A structural basis for 14-3-3sigma functional specificity.

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

The functional interaction of 14-3-3 proteins with the ERK1/2 scaffold KSR1 occurs in an isoform-specific manner

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Bimodal regulation of FoxO3 by AKT and 14-3-3

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Chibby cooperates with 14-3-3 to regulate beta-catenin subcellular distribution and signaling activity

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

An integrin-alpha4-14-3-3zeta-paxillin ternary complex mediates localised Cdc42 activity and accelerates cell migration

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

14-3-3 proteins mediate an essential anti-apoptotic signal

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

BCR kinase phosphorylates 14-3-3 Tau on residue 233.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Role of tau protein in both physiological and pathological conditions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

A novel sphingosine-dependent protein kinase (SDK1) specifically phosphorylates certain isoforms of 14-3-3 protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified as the kinase domain of protein kinase C delta

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Identification of 14-3-3zeta as a protein kinase B/Akt substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Sphingosine and FTY720 directly bind pro-survival 14-3-3 proteins to regulate their function.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Arachidonic acid binds 14-3-3zeta, releases 14-3-3zeta from phosphorylated BAD and induces aggregation of 14-3-3zeta

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

A novel ligand-binding site in the zeta-form 14-3-3 protein recognizing the platelet glycoprotein Ibalpha and distinct from the c-Raf-binding site.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

The 14-3-3 protein binds its target proteins with a common site located towards the C-terminus

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Properties of the monomeric form of human 14-3-3ζ protein and its interaction with tau and HspB6.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Dimerization is essential for 14-3-3zeta stability and function in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.10.048

10.1016/J.FEBSLET.2012.10.048

21 January 2018

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28 August 2017

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