(Q36658598)

English

Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectively

scientific article published on January 1993

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scholarly article

1 reference

Europe PubMed Central

15 August 2017

Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectively (English)

1 reference

Europe PubMed Central

15 August 2017

phosphorylation

1 reference

based on heuristic

inferred from title

Mindaugas Valius

1

1 reference

Europe PubMed Central

15 August 2017

author name string

C Bazenet

2

1 reference

Europe PubMed Central

15 August 2017

A Kazlauskas

3

1 reference

Europe PubMed Central

15 August 2017

language of work or name

0 references

publication date

1 January 1993

1 reference

Europe PubMed Central

15 August 2017

Molecular and Cellular Biology

1 reference

Europe PubMed Central

15 August 2017

13

1 reference

Europe PubMed Central

15 August 2017

133-143

1 reference

Europe PubMed Central

15 August 2017

1

1 reference

Europe PubMed Central

15 August 2017

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Improved retroviral vectors for gene transfer and expression

1 reference

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Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C

1 reference

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Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-gamma in quiescent BALB/c 3T3 cells

1 reference

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Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins

1 reference

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Two different subunits associate to create isoform-specific platelet-derived growth factor receptors

1 reference

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Signal transduction by the platelet-derived growth factor receptor

1 reference

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Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody

1 reference

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Mutations of the platelet-derived growth factor receptor that cause a loss of ligand-induced conformational change, subtle changes in kinase activity, and impaired ability to stimulate DNA synthesis

1 reference

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Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro

1 reference

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Role of phosphatidylinositol kinase in PDGF receptor signal transduction

1 reference

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Different effects of homo- and heterodimers of platelet-derived growth factor A and B chains on human and mouse fibroblasts

1 reference

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Protein kinase C mediates platelet-derived growth factor-induced tyrosine phosphorylation of p42.

1 reference

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Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors

1 reference

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Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Binding of GAP to activated PDGF receptors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Platelet-derived growth factor: mechanism of action and possible in vivo function

1 reference

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Oncogenes and signal transduction

1 reference

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A site of tyrosine phosphorylation in the C terminus of the epidermal growth factor receptor is required to activate phospholipase C.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner

1 reference

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

1 reference

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

1 reference

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A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Platelet-derived growth factor receptor sequences important for binding of src family tyrosine kinases

1 reference

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A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Functions of the major tyrosine phosphorylation site of the PDGF receptor beta subunit

1 reference

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Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction

1 reference

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SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma

1 reference

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Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis

1 reference

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GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit

1 reference

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Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways

1 reference

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SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors

1 reference

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Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors

1 reference

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1 reference

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Tyr721 regulates specific binding of the CSF-1 receptor kinase insert to PI 3'-kinase SH2 domains: a model for SH2-mediated receptor-target interactions

1 reference

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The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor

1 reference

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Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor

1 reference

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PDGF beta-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex

1 reference

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Regulation of Phospholipase C-γ1 by Profilin and Tyrosine Phosphorylation

1 reference

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PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation

1 reference

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Association between the PDGF receptor and members of the src family of tyrosine kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=358893

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Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis

1 reference

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PDGF-induced activation of phospholipase C is not required for induction of DNA synthesis

1 reference

https://pubmed.ncbi.nlm.nih.gov/7678051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/MCB.13.1.133

1 reference

Europe PubMed Central

15 August 2017

1 reference

Europe PubMed Central

15 August 2017

1 reference

Europe PubMed Central

15 August 2017

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