Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell Signaling

Lu, Wei; Gong, Delquin; Bar-Sagi, Dafna; Cole, Philip A

doi:10.1016/s1097-2765(01)00369-0

Cited by 269Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingCytokine Signaling Pathways and Interactions

Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell Signaling

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Lu, Wei, Gong, Delquin, Bar-Sagi, Dafna, Cole, Philip A·2001·Molecular Cell

DOI 10.1016/s1097-2765(01)00369-0

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Abstract

The regulation of protein tyrosine phosphatase (PTPase) SHP-2 is proposed to involve tyrosine phosphorylation on two tail tyrosine residues. Using "expressed protein ligation", nonhydrolyzable phosphotyrosine analogs were introduced at known phosphorylation sites in SHP-2. Biochemical analysis suggests that a phosphonate at Tyr542 interacts intramolecularly with the N-terminal SH2 domain to relieve basal inhibition of the PTPase, whereas a phosphonate at Tyr-580 stimulates the PTPase activity by interaction with the C-terminal SH2 domain. Microinjection experiments indicate that a single phosphorylation of Tyr-542 of SHP-2 is sufficient to activate the MAP kinase pathway in living cells. These studies support a novel mechanism explaining how tyrosine phosphorylation of a PTPase is important in signal transduction.

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The lack of influence of SHP2 on robustness of late IL-6-induced STAT3 activation might be explained by the fact that SHP2 itself is phosphorylated rapidly in response to IL-6, which causes dissociation from gp130.
“The lack of influence of SHP2 on robustness of late IL-6-induced STAT3 activation (Fig. 4) might be explained by the fact that SHP2 itself is phosphorylated rapidly in response to IL-6 (Fig. 1b) which causes dissociation from gp130 [9–11].”
From The tyrosine phosphatase SHP2 increases robustness and information transfer within IL-6-induced JAK/STAT signalling (2021) · cites this paper as [9]

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Authors: Lu, W., Gong, D., Bar-Sagi, D., & Cole, P. A.
Affiliations: State University of New York (US)
Johns Hopkins University (US)
Corresponding author: Cole, Philip A
ORCID: Gong, Delquin
Cole, Philip A
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2001-10
Volume: 8
Issue: 4
Pages: 759-769
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(01)00369-0
OpenAlex: W2000348274
Cited by: 268
References: 57
Citations by year: 2026: 7 · 2025: 7 · 2024: 5 · 2023: 8 · 2022: 16 · 2021: 11 · 2020: 13 · 2019: 4 · 2018: 3 · 2017: 11 · 2016: 6 · 2015: 10 · 2014: 8 · 2013: 13 · 2012: 15
FWCI: 4.20
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4307 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Burroughs Wellcome Fund
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords: SHP2, tyrosine phosphorylation, phosphotyrosine mimetics, expressed protein ligation, protein tyrosine phosphatase, SH2 domain, MAPK signaling, signal transduction, phosphonate analogs, enzyme activation
MeSH terms: Amino Acid Sequence, Enzyme Activation, Microinjections, Microscopy, Fluorescence, Molecular Sequence Data, Phosphorylation, Protein Conformation, Proteins, Recombinant Fusion Proteins, Molecular Structure, Signal Transduction, Culture Media, Serum-Free, Protein Tyrosine Phosphatases, Point Mutation, Phosphotyrosine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Subtilisin, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases

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Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell Signaling

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