Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2

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Standard

Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. / VanderKuur, J; Allevato, G; Billestrup, Nils; Norstedt, G; Carter-Su, C.

I: The Journal of Biological Chemistry, Bind 270, Nr. 13, 31.03.1995, s. 7587-93.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

VanderKuur, J, Allevato, G, Billestrup, N, Norstedt, G & Carter-Su, C 1995, 'Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2', The Journal of Biological Chemistry, bind 270, nr. 13, s. 7587-93.

APA

VanderKuur, J., Allevato, G., Billestrup, N., Norstedt, G., & Carter-Su, C. (1995). Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. The Journal of Biological Chemistry, 270(13), 7587-93.

Vancouver

VanderKuur J, Allevato G, Billestrup N, Norstedt G, Carter-Su C. Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. The Journal of Biological Chemistry. 1995 mar 31;270(13):7587-93.

Author

VanderKuur, J ; Allevato, G ; Billestrup, Nils ; Norstedt, G ; Carter-Su, C. / Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2. I: The Journal of Biological Chemistry. 1995 ; Bind 270, Nr. 13. s. 7587-93.

Bibtex

@article{138e7198ffd14b71821a3de21cca5f5a,
title = "Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2",
abstract = "Growth hormone (GH) has been shown to stimulate the mitogen-activated protein (MAP) kinases designated ERKs (extracellular signal regulated kinases) 1 and 2. One pathway by which ERKs 1 and 2 are activated by tyrosine kinases involves the Src homology (SH)-2 containing proteins SHC and Grb2. To gain insight into pathways coupling GH receptor (GHR) to MAP kinase activation and signaling molecules that might interact with GHR and its associated tyrosine kinase JAK2, we examined whether SHC and Grb2 proteins serve as signaling molecules for GH. Human GH was shown to promote the rapid tyrosyl phosphorylation of 66-, 52-, and 46-kDa SHC proteins in 3T3-F442A fibroblasts. GH also promoted binding of GHR and JAK2 to the SH2 domain of 46/52-kDa SHC protein fused to glutathione S-transferase (GST). Constitutively phosphorylated JAK2, from COS-7 cells transiently transfected with murine JAK2 cDNA, bound to SHC SH2-GST fusion protein, demonstrating that the SHC SH2 domain can bind tyrosyl-phosphorylated JAK2 in the absence of GHR. Regions of GHR required for GH-dependent tyrosyl phosphorylation of SHC were examined using Chinese hamster ovary cells expressing mutated rat GHR. In cells expressing GHR1-638 and GHR1-638(Y333,338F), GH stimulated phosphorylation of all 3 SHC proteins whereas GH stimulated phosphorylation of only the 66- and 52-kDa SHC proteins in cells expressing GHR1-454. GH had no effect on SHC phosphorylation in cells expressing GHR1-294 or GHR delta P, the latter lacking amino acids 297-311 containing the proline-rich motif required for JAK2 activation by GH. In contrast to SHC, Grb2 appeared not to interact directly with GHR or JAK2. However, Grb2 was shown to associate rapidly with SHC proteins in a GH-dependent manner. These findings suggest that GH stimulates: 1) the association of SHC proteins with JAK2.GHR complexes via the SHC-SH2 domain, 2) tyrosyl phosphorylation of SHC proteins, and 3) subsequent Grb2 association with SHC proteins. These events are likely to be early events in GH activation of MAP kinases and possibly of other responses to GH.",
keywords = "3T3 Cells, Adaptor Proteins, Signal Transducing, Animals, Calcium-Calmodulin-Dependent Protein Kinases, Cell Line, Cercopithecus aethiops, Electrophoresis, Polyacrylamide Gel, GRB2 Adaptor Protein, Growth Hormone, Humans, Janus Kinase 2, Kidney, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Mutagenesis, Site-Directed, Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Rats, Receptor, Epidermal Growth Factor, Receptors, Somatotropin, Recombinant Proteins, Transfection, Tyrosine",
author = "J VanderKuur and G Allevato and Nils Billestrup and G Norstedt and C Carter-Su",
year = "1995",
month = mar,
day = "31",
language = "English",
volume = "270",
pages = "7587--93",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "13",

}

RIS

TY - JOUR

T1 - Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2

AU - VanderKuur, J

AU - Allevato, G

AU - Billestrup, Nils

AU - Norstedt, G

AU - Carter-Su, C

PY - 1995/3/31

Y1 - 1995/3/31

N2 - Growth hormone (GH) has been shown to stimulate the mitogen-activated protein (MAP) kinases designated ERKs (extracellular signal regulated kinases) 1 and 2. One pathway by which ERKs 1 and 2 are activated by tyrosine kinases involves the Src homology (SH)-2 containing proteins SHC and Grb2. To gain insight into pathways coupling GH receptor (GHR) to MAP kinase activation and signaling molecules that might interact with GHR and its associated tyrosine kinase JAK2, we examined whether SHC and Grb2 proteins serve as signaling molecules for GH. Human GH was shown to promote the rapid tyrosyl phosphorylation of 66-, 52-, and 46-kDa SHC proteins in 3T3-F442A fibroblasts. GH also promoted binding of GHR and JAK2 to the SH2 domain of 46/52-kDa SHC protein fused to glutathione S-transferase (GST). Constitutively phosphorylated JAK2, from COS-7 cells transiently transfected with murine JAK2 cDNA, bound to SHC SH2-GST fusion protein, demonstrating that the SHC SH2 domain can bind tyrosyl-phosphorylated JAK2 in the absence of GHR. Regions of GHR required for GH-dependent tyrosyl phosphorylation of SHC were examined using Chinese hamster ovary cells expressing mutated rat GHR. In cells expressing GHR1-638 and GHR1-638(Y333,338F), GH stimulated phosphorylation of all 3 SHC proteins whereas GH stimulated phosphorylation of only the 66- and 52-kDa SHC proteins in cells expressing GHR1-454. GH had no effect on SHC phosphorylation in cells expressing GHR1-294 or GHR delta P, the latter lacking amino acids 297-311 containing the proline-rich motif required for JAK2 activation by GH. In contrast to SHC, Grb2 appeared not to interact directly with GHR or JAK2. However, Grb2 was shown to associate rapidly with SHC proteins in a GH-dependent manner. These findings suggest that GH stimulates: 1) the association of SHC proteins with JAK2.GHR complexes via the SHC-SH2 domain, 2) tyrosyl phosphorylation of SHC proteins, and 3) subsequent Grb2 association with SHC proteins. These events are likely to be early events in GH activation of MAP kinases and possibly of other responses to GH.

AB - Growth hormone (GH) has been shown to stimulate the mitogen-activated protein (MAP) kinases designated ERKs (extracellular signal regulated kinases) 1 and 2. One pathway by which ERKs 1 and 2 are activated by tyrosine kinases involves the Src homology (SH)-2 containing proteins SHC and Grb2. To gain insight into pathways coupling GH receptor (GHR) to MAP kinase activation and signaling molecules that might interact with GHR and its associated tyrosine kinase JAK2, we examined whether SHC and Grb2 proteins serve as signaling molecules for GH. Human GH was shown to promote the rapid tyrosyl phosphorylation of 66-, 52-, and 46-kDa SHC proteins in 3T3-F442A fibroblasts. GH also promoted binding of GHR and JAK2 to the SH2 domain of 46/52-kDa SHC protein fused to glutathione S-transferase (GST). Constitutively phosphorylated JAK2, from COS-7 cells transiently transfected with murine JAK2 cDNA, bound to SHC SH2-GST fusion protein, demonstrating that the SHC SH2 domain can bind tyrosyl-phosphorylated JAK2 in the absence of GHR. Regions of GHR required for GH-dependent tyrosyl phosphorylation of SHC were examined using Chinese hamster ovary cells expressing mutated rat GHR. In cells expressing GHR1-638 and GHR1-638(Y333,338F), GH stimulated phosphorylation of all 3 SHC proteins whereas GH stimulated phosphorylation of only the 66- and 52-kDa SHC proteins in cells expressing GHR1-454. GH had no effect on SHC phosphorylation in cells expressing GHR1-294 or GHR delta P, the latter lacking amino acids 297-311 containing the proline-rich motif required for JAK2 activation by GH. In contrast to SHC, Grb2 appeared not to interact directly with GHR or JAK2. However, Grb2 was shown to associate rapidly with SHC proteins in a GH-dependent manner. These findings suggest that GH stimulates: 1) the association of SHC proteins with JAK2.GHR complexes via the SHC-SH2 domain, 2) tyrosyl phosphorylation of SHC proteins, and 3) subsequent Grb2 association with SHC proteins. These events are likely to be early events in GH activation of MAP kinases and possibly of other responses to GH.

KW - 3T3 Cells

KW - Adaptor Proteins, Signal Transducing

KW - Animals

KW - Calcium-Calmodulin-Dependent Protein Kinases

KW - Cell Line

KW - Cercopithecus aethiops

KW - Electrophoresis, Polyacrylamide Gel

KW - GRB2 Adaptor Protein

KW - Growth Hormone

KW - Humans

KW - Janus Kinase 2

KW - Kidney

KW - Mice

KW - Mitogen-Activated Protein Kinase 1

KW - Mitogen-Activated Protein Kinase 3

KW - Mitogen-Activated Protein Kinases

KW - Mutagenesis, Site-Directed

KW - Phosphoproteins

KW - Phosphorylation

KW - Phosphotyrosine

KW - Protein-Tyrosine Kinases

KW - Proteins

KW - Proto-Oncogene Proteins

KW - Rats

KW - Receptor, Epidermal Growth Factor

KW - Receptors, Somatotropin

KW - Recombinant Proteins

KW - Transfection

KW - Tyrosine

M3 - Journal article

C2 - 7535773

VL - 270

SP - 7587

EP - 7593

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 13

ER -

ID: 132900469