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Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
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364751
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23 October 2019
title
Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor
(English)
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364751
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23 October 2019
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Anna Mondino
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4
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23 October 2019
Joseph Schlessinger
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J Schlessinger
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364751
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23 October 2019
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R Nishimura
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23 October 2019
W Li
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23 October 2019
A Kashishian
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3
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23 October 2019
M Zhou
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5
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23 October 2019
J Cooper
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6
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23 October 2019
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1 November 1993
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23 October 2019
published in
Molecular and Cellular Biology
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23 October 2019
volume
13
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23 October 2019
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11
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364751
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23 October 2019
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6889-6896
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364751
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23 October 2019
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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
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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
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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
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The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment
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Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma
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Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulation
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GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit
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The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors
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Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP
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The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms
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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
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Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
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SH2 domains recognize specific phosphopeptide sequences
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Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
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Phospholipase C-gamma 1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
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Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins
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Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
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Phosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase C gamma 1
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Oncogenes and signal transduction
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Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
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7 April 2017
C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains
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7 April 2017
Growth factor signaling by receptor tyrosine kinases
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7 April 2017
Signalling through SH2 and SH3 domains
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27 September 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
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
Structural features of the colony-stimulating factor 1 receptor that affect its association with phosphatidylinositol 3-kinase
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27 September 2017
Deletion or substitution within the alpha platelet-derived growth factor receptor kinase insert domain: effects on functional coupling with intracellular signaling pathways
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reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
Mutagenic analysis of the v-crk oncogene: requirement for SH2 and SH3 domains and correlation between increased cellular phosphotyrosine and transformation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
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
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors
1 reference
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reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
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27 September 2017
The SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
27 September 2017
Deletion of the kinase insert sequence of the platelet-derived growth factor beta-receptor affects receptor kinase activity and signal transduction
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
30 May 2018
Tyrosine phosphorylation of a common 57-kDa protein in growth factor-stimulated and -transformed cells
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
30 May 2018
Analysis of platelet-derived growth factor receptor domain function using a novel chimeric receptor approach.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
30 May 2018
Transduction of circular membrane ruffling by the platelet-derived growth factor beta-receptor is dependent on its kinase insert
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
30 May 2018
Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
30 May 2018
A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=364751
retrieved
29 November 2018
Identifiers
DOI
10.1128/MCB.13.11.6889
1 reference
stated in
Europe PubMed Central
PMC publication ID
364751
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7692233%20AND%20SRC:MED&resulttype=core&format=json
retrieved
23 October 2019
PMC publication ID
364751
1 reference
stated in
Europe PubMed Central
PMC publication ID
364751
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7692233%20AND%20SRC:MED&resulttype=core&format=json
retrieved
23 October 2019
PubMed publication ID
7692233
1 reference
stated in
Europe PubMed Central
PMC publication ID
364751
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7692233%20AND%20SRC:MED&resulttype=core&format=json
retrieved
23 October 2019
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