Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors

Bjørbæk, Christian; Buchholz, Ryan M.; Davis, Sarah M.; Bates, Sarah H.; Pierroz, Dominique D.; Gu, Haihua; Neel, Benjamin G.; Myers, Martin G.; Flier, Jeffrey S.

doi:10.1074/jbc.m007439200

Cited by 364Protein Tyrosine PhosphatasesRegulation of Appetite and ObesityCytokine Signaling Pathways and Interactions

Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors

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Bjørbæk, Christian, Buchholz, Ryan M., Davis, Sarah M., Bates, Sarah H., Pierroz, Dominique D., Gu, Haihua, Neel, Benjamin G., Myers, Martin G. +1 more·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m007439200

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Abstract

The protein tyrosine phosphatase SHP-2 has been proposed to serve as a regulator of leptin signaling, but its specific roles are not fully examined. To directly investigate the role of SHP-2, we employed dominant negative strategies in transfected cells. We show that a catalytically inactive mutant of SHP-2 blocks leptin-stimulated ERK phosphorylation by the long leptin receptor, ObRb. SHP-2, lacking two C-terminal tyrosine residues, partially inhibits ERK phosphorylation. We find similar effects of the SHP-2 mutants after examining stimulation of an ERK-dependent egr-1 promoter-construct by leptin. We also demonstrate ERK phosphorylation and egr-1 mRNA expression in the hypothalamus by leptin. Analysis of signaling by ObRb lacking intracellular tyrosine residues or by the short leptin receptor, ObRa, enabled us to conclude that two pathways are critical for ERK activation. One pathway does not require the intracellular domain of ObRb, whereas the other pathway requires tyrosine residue 985 of ObRb. The phosphatase activity of SHP-2 is required for both pathways, whereas activation of ERK via Tyr-985 of ObRb also requires tyrosine phosphorylation of SHP-2. SHP-2 is thus a positive regulator of ERK by leptin receptors, and both the adaptor function and the phosphatase activity of SHP-2 are critical for this regulation.

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Phosphorylation of Tyr985 recruits SHP-2 to LepRb, leading to ERK pathway activation in cultured cells and recruitment of SOCS-3.
“Phosphorylation of Tyr985 recruits SH2-domain-containing phosphatase-2 (SHP-2) to LepRb, leading to the activation of the extracellular signal regulated (ERK) signaling pathway in cultured cells, as well as the recruitment of suppressor of cytokine signaling-3 (SOCS-3), a negative regulator of LepRb signaling (6, 21, 22).”
From Leptin and the Central Nervous System Control of Glucose Metabolism (2011) · cites this paper as [21]

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“Phosphorylation of Tyr985 recruits SH2 domain-containing phosphatase-2 (SHP-2) to LepRb, leading to the activation of the extracellular signal regulated (ERK) signaling pathway in cultured cells, as well as the recruitment of suppressor of cytokine signaling-3 (SOCS-3), a negative regulator of LepRb signaling (6, 21,…”
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Authors: Bjørbæk, C., Buchholz, R. M., Davis, S. M., Bates, S. H., Pierroz, D. D., Gu, H., Neel, B. G., Myers, M. G., & Flier, J. S.
Affiliations: Beth Israel Deaconess Medical Center (US)
Joslin Diabetes Center (US)
Corresponding author: Flier, Jeffrey S.
ORCID: Pierroz, Dominique D.
Gu, Haihua
Neel, Benjamin G.
Myers, Martin G.
Flier, Jeffrey S.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2001-02
Volume: 276
Issue: 7
Pages: 4747-4755
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m007439200
OpenAlex: W2123126462
Semantic Scholar: 611dde37fd76b46071411d3b23e750b6a97b4a24
Cited by: 364
References: 63
Citations by year: 2026: 3 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 4 · 2021: 9 · 2020: 10 · 2019: 5 · 2018: 12 · 2017: 14 · 2016: 9 · 2015: 12 · 2014: 25 · 2013: 17 · 2012: 19
FWCI: 8.28
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7191 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01-CA-49152, F32CA072144, R01CA049152, CA72144)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK050693, DK-50693, DK-R37-28082, R37DK028082, R01-DK-56731, R01DK056731)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Regulation of Appetite and Obesity
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords: SHP2, leptin receptor, ERK activation, Obras, protein tyrosine phosphatase, EGR1, leptin signaling, tyrosine phosphorylation, dominant-negative mutant, hypothalamus, receptor tyrosine kinase signaling
MeSH terms: Animals, Carrier Proteins, DNA-Binding Proteins, Cricetinae, Hypothalamus, Male, Mice, Inbred C57BL, Models, Biological, Mutation, Phosphorylation, Promoter Regions, Genetic, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Receptors, Cell Surface, RNA, Messenger, Transcription Factors, Transcription, Genetic, Transfection, Trans-Activators, CHO Cells, Protein Tyrosine Phosphatases, Immediate-Early Proteins, Leptin, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Intracellular Signaling Peptides and Proteins, Mitogen-Activated Protein Kinase 3, STAT3 Transcription Factor, Mice, Early Growth Response Protein 1, Janus Kinase 2, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Receptors, Leptin, Protein Tyrosine Phosphatase, Non-Receptor Type 11

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Divergent Roles of SHP-2 in ERK Activation by Leptin Receptors

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