Catalytically active membrane-distal phosphatase domain of receptor protein-tyrosine phosphatase alpha is required for Src activation (Q24299290)

Protein tyrosine phosphatases in the human genome

GOA release 2020-03-11

author name string

Andrei M Vacaru

series ordinal

1

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Jeroen den Hertog

series ordinal

2

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language of work or name

English

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publication date

March 2010

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published in

FEBS Journal

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volume

277

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page(s)

1562-70

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issue

6

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cites work

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The structure of the membrane distal phosphatase domain of RPTPalpha reveals interdomain flexibility and an SH2 domain interaction region

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Purification and characterization of the cytoplasmic domain of human receptor-like protein tyrosine phosphatase RPTP mu

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Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase alpha.

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The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma

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Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs

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The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains

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Involvement of the membrane distal catalytic domain in pervanadate-induced tyrosine phosphorylation of receptor protein-tyrosine phosphatase alpha.

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A phosphotyrosine displacement mechanism for activation of Src by PTPalpha

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Interconversion of the kinetic identities of the tandem catalytic domains of receptor-like protein-tyrosine phosphatase PTPalpha by two point mutations is synergistic and substrate-dependent.

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Catalytic activation of the membrane distal domain of protein tyrosine phosphatase ϵ, but not CD45, by two point mutations

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7 January 2021

Anti-phosphatases take the stage

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7 January 2021

Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase alpha

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The second domain of the CD45 protein tyrosine phosphatase is critical for interleukin-2 secretion and substrate recruitment of TCR-zeta in vivo

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7 January 2021