Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation (Q28141661)

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3 November 2019

title

Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation (English)

1 reference

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3 November 2019

author name string

Y J Jin

series ordinal

2

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3 November 2019

language of work or name

English

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publication date

1 January 2000

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Journal of Biological Chemistry

3 November 2019

published in

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3 November 2019

volume

275

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3 November 2019

issue

1

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3 November 2019

page(s)

599-604

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STATs and Gene Regulation

3 November 2019

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Cloning and expression of Stat5 and an additional homologue (Stat5b) involved in prolactin signal transduction in mouse mammary tissue

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Stat5a is mandatory for adult mammary gland development and lactogenesis.

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Requirement of STAT5b for sexual dimorphism of body growth rates and liver gene expression

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Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses

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Stat5b is essential for natural killer cell-mediated proliferation and cytolytic activity

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Stat5 is required for IL-2-induced cell cycle progression of peripheral T cells

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Constitutively Activated Jak-STAT Pathway in T Cells Transformed with HTLV-I

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Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation.

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Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein

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CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling

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SOCS-3 is tyrosine phosphorylated in response to interleukin-2 and suppresses STAT5 phosphorylation and lymphocyte proliferation

21 January 2018

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Evidence for a physical association between the Shc-PTB domain and the beta c chain of the granulocyte-macrophage colony-stimulating factor receptor

21 January 2018

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Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation

21 January 2018

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Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells.

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A functional DNA binding domain is required for growth hormone-induced nuclear accumulation of Stat5B.

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Nucleocytoplasmic transport: the soluble phase

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Induction of S-Phase Entry by E2F Transcription Factors Depends on Their Nuclear Localization

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MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo

21 January 2018

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Lack of SHPTP1 results in src-family kinase hyperactivation and thymocyte hyperresponsiveness

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Examination of the potential functional role of conserved cysteine residues in the hormone binding domain of the human 1,25-dihydroxyvitamin D3 receptor.

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Amino-terminal signal transducer and activator of transcription (STAT) domains regulate nuclear translocation and STAT deactivation.

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Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1.

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Cytokine-receptor complexes as chaperones for nuclear translocation of signal transducers.

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Positive Effects of SH2 Domain-containing Tyrosine Phosphatase SHP-1 on Epidermal Growth Factor- and Interferon-γ-stimulated Activation of STAT Transcription Factors in HeLa Cells

21 January 2018

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The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression

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Dual signaling role of the protein tyrosine phosphatase SHP-2 in regulating expression of acute-phase plasma proteins by interleukin-6 cytokine receptors in hepatic cells.

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Anopheles gambiae Ag-STAT, a new insect member of the STAT family, is activated in response to bacterial infection

21 January 2018

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Characterization of a Stat-like DNA binding activity in Drosophila melanogaster.

21 January 2018

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Regulation of Interferon-α Responsiveness by the Duration of Janus Kinase Activity

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Interaction of Growth Hormone-activated STATs with SH2-containing Phosphotyrosine Phosphatase SHP-1 and Nuclear JAK2 Tyrosine Kinase

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.275.1.599

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10617656%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017