14-3-3zeta is an effector of tau protein phosphorylation (Q22254233)

PubMed

8 February 2023

K Sobue

series ordinal

author given names

author last names

Sobue

1 reference

PubMed

8 February 2023

H K Paudel

series ordinal

author given names

H K

author last names

Paudel

1 reference

PubMed

Journal of Biological Chemistry

8 February 2023

language of work or name

English

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publication date

18 August 2000

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published in

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volume

275

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issue

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page(s)

25247-54

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cites work

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Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms

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Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

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14-3-3 and its possible role in co-ordinating multiple signalling pathways

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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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Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa

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Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa.

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

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

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Oligomerization activates c-Raf-1 through a Ras-dependent mechanism

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Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration

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The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding

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Phosphorylation of tau protein by casein kinase-1 converts it to an abnormal Alzheimer-like state.

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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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Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease

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14-3-3 proteins associate with cdc25 phosphatases

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Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

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

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14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner

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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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Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau.

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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.

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Reversal of Raf-1 Activation by Purified and Membrane-Associated Protein Phosphatases

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Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family

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Association of polyomavirus middle tumor antigen with 14-3-3 proteins

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

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cAMP-dependent protein kinase phosphorylations on tau in Alzheimer's disease.

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Identifiers

DOI

10.1074/JBC.M003738200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017