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Forside

Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein. / Goldberg, Y; Glineur, C; Gesquière, J C; Ricouart, A; Sap, J; Vennström, B; Ghysdael, J.

I: EMBO Journal, Bind 7, Nr. 8, 1988, s. 2425-33.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Goldberg, Y, Glineur, C, Gesquière, JC, Ricouart, A, Sap, J, Vennström, B & Ghysdael, J 1988, 'Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein.', EMBO Journal, bind 7, nr. 8, s. 2425-33.

APA

Goldberg, Y., Glineur, C., Gesquière, J. C., Ricouart, A., Sap, J., Vennström, B., & Ghysdael, J. (1988). Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein. EMBO Journal, 7(8), 2425-33.

Vancouver

Goldberg Y, Glineur C, Gesquière JC, Ricouart A, Sap J, Vennström B o.a. Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein. EMBO Journal. 1988;7(8):2425-33.

Author

Goldberg, Y ; Glineur, C ; Gesquière, J C ; Ricouart, A ; Sap, J ; Vennström, B ; Ghysdael, J. / Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein. I: EMBO Journal. 1988 ; Bind 7, Nr. 8. s. 2425-33.

Bibtex

@article{5d0f6bb054ad11dd8d9f000ea68e967b,
title = "Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein.",
abstract = "The c-erbA proto-oncogene encodes a nuclear receptor for thyroid hormone (T3), which is believed to stimulate transcription from specific target promoters upon binding to cis-acting DNA sequence elements. The v-erbA oncogene of avian erythroblastosis virus (AEV) encodes a ligand-independent version of this nuclear receptor. The v-erbA product inhibits terminal differentiation of avian erythroblasts, presumably by affecting the transcription of specific genes. We show here that the c-erbA-encoded nuclear receptor (p46c-erbA) is phosphorylated on serine residues on two distinct sites. One of these sites, defined by the limit tryptic phosphopeptide 28SSQCLVK, is retained on the v-erbA-encoded P75gag-v-erbA protein. This site is located in the amino-terminal domain of these molecules, 21 amino acids upstream of the DNA-binding region. Phosphorylation of this site in both p46c-erbA and P75gag-v-erbA is enhanced 10-fold following treatment of cells with activators of either protein kinase C or cAMP-dependent protein kinase. Since cAMP-dependent protein kinase phosphorylates both p46c-erbA and P75gag-v-erbA in vitro at the same site as that observed in vivo, at least part of the cAMP-dependent phosphorylation of erbA molecules in cells could result from direct phosphorylation by this enzyme. The possible role phosphorylation may play in the function of the erbA-encoded transcriptional factors is discussed.",
author = "Y Goldberg and C Glineur and Gesqui{\`e}re, {J C} and A Ricouart and J Sap and B Vennstr{\"o}m and J Ghysdael",
note = "Keywords: Alpharetrovirus; Animals; Base Sequence; Cell Line, Transformed; Chick Embryo; Enzyme Activation; Gene Expression Regulation; Oncogene Proteins v-erbA; Peptide Fragments; Peptide Mapping; Phosphorylation; Precipitin Tests; Protein Kinase C; Protein Kinases; Proto-Oncogene Proteins; Proto-Oncogenes; Receptors, Thyroid Hormone; Retroviridae Proteins",
year = "1988",
language = "English",
volume = "7",
pages = "2425--33",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "8",

}

RIS

TY - JOUR

T1 - Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein.

AU - Goldberg, Y

AU - Glineur, C

AU - Gesquière, J C

AU - Ricouart, A

AU - Sap, J

AU - Vennström, B

AU - Ghysdael, J

N1 - Keywords: Alpharetrovirus; Animals; Base Sequence; Cell Line, Transformed; Chick Embryo; Enzyme Activation; Gene Expression Regulation; Oncogene Proteins v-erbA; Peptide Fragments; Peptide Mapping; Phosphorylation; Precipitin Tests; Protein Kinase C; Protein Kinases; Proto-Oncogene Proteins; Proto-Oncogenes; Receptors, Thyroid Hormone; Retroviridae Proteins

PY - 1988

Y1 - 1988

N2 - The c-erbA proto-oncogene encodes a nuclear receptor for thyroid hormone (T3), which is believed to stimulate transcription from specific target promoters upon binding to cis-acting DNA sequence elements. The v-erbA oncogene of avian erythroblastosis virus (AEV) encodes a ligand-independent version of this nuclear receptor. The v-erbA product inhibits terminal differentiation of avian erythroblasts, presumably by affecting the transcription of specific genes. We show here that the c-erbA-encoded nuclear receptor (p46c-erbA) is phosphorylated on serine residues on two distinct sites. One of these sites, defined by the limit tryptic phosphopeptide 28SSQCLVK, is retained on the v-erbA-encoded P75gag-v-erbA protein. This site is located in the amino-terminal domain of these molecules, 21 amino acids upstream of the DNA-binding region. Phosphorylation of this site in both p46c-erbA and P75gag-v-erbA is enhanced 10-fold following treatment of cells with activators of either protein kinase C or cAMP-dependent protein kinase. Since cAMP-dependent protein kinase phosphorylates both p46c-erbA and P75gag-v-erbA in vitro at the same site as that observed in vivo, at least part of the cAMP-dependent phosphorylation of erbA molecules in cells could result from direct phosphorylation by this enzyme. The possible role phosphorylation may play in the function of the erbA-encoded transcriptional factors is discussed.

AB - The c-erbA proto-oncogene encodes a nuclear receptor for thyroid hormone (T3), which is believed to stimulate transcription from specific target promoters upon binding to cis-acting DNA sequence elements. The v-erbA oncogene of avian erythroblastosis virus (AEV) encodes a ligand-independent version of this nuclear receptor. The v-erbA product inhibits terminal differentiation of avian erythroblasts, presumably by affecting the transcription of specific genes. We show here that the c-erbA-encoded nuclear receptor (p46c-erbA) is phosphorylated on serine residues on two distinct sites. One of these sites, defined by the limit tryptic phosphopeptide 28SSQCLVK, is retained on the v-erbA-encoded P75gag-v-erbA protein. This site is located in the amino-terminal domain of these molecules, 21 amino acids upstream of the DNA-binding region. Phosphorylation of this site in both p46c-erbA and P75gag-v-erbA is enhanced 10-fold following treatment of cells with activators of either protein kinase C or cAMP-dependent protein kinase. Since cAMP-dependent protein kinase phosphorylates both p46c-erbA and P75gag-v-erbA in vitro at the same site as that observed in vivo, at least part of the cAMP-dependent phosphorylation of erbA molecules in cells could result from direct phosphorylation by this enzyme. The possible role phosphorylation may play in the function of the erbA-encoded transcriptional factors is discussed.

M3 - Journal article

C2 - 2903825

VL - 7

SP - 2425

EP - 2433

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 8

ER -

ID: 5070218