Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle

Autores
Banchio, Claudia Elena; Schang, Luis M.; Vance, Dennis E.
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Phosphatidylcholine is the major lipid component in mammalian membranes. Phosphatidylcholine synthesis increases in C3H10T1/2 fibroblasts during the G1 and S phases of the cell cycle. Previous studies demonstrated that the mRNA encoding CTP:phosphocholine cytidylyltransferase (CT ) increases during S phase (Golfman, L. S., Bakovic, M., and Vance, D. E. (2001) J. Biol. Chem. 276, 43688–43692) and that this activation is driven by increased binding of Sp1 to the CT promoter (Banchio, C., Schang, L. M., and Vance, D. E. (2003) J. Biol. Chem. 278, 32457–32464). We now demonstrate that cyclin-dependent kinase 2 (CDK2) phosphorylation of Sp1 activates CT transcription during S phase. Sp1 binds in a phosphorylated state to the CT promoter. Sp1 binding is enhanced by association with cyclin A/E and CDK2, both in vivo and in vitro. In cells that overexpress Sp1, co-expression of cyclin A and CDK2 induces a high and constant level of CT expression, whereas reduction in the expression of cyclin A, cyclin E, and CDK2 eliminates the induction of CT expression in S phase. Furthermore, CT expression is decreased in cells overexpressing a dominant-negative form of CDK2 and in cells treated with the CDK2 kinase inhibitors roscovitine and olomoucine. These results enhance our understanding of the regulatory mechanisms involved in the expression of CT in preparation for cell division.
Fil: Banchio, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Schang, Luis M.. University of Alberta; Canadá
Fil: Vance, Dennis E.. University of Alberta; Canadá
Materia
Phosphorylation
CTP
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/185571

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network_name_str CONICET Digital (CONICET)
spelling Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell CycleBanchio, Claudia ElenaSchang, Luis M.Vance, Dennis E.PhosphorylationCTPhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Phosphatidylcholine is the major lipid component in mammalian membranes. Phosphatidylcholine synthesis increases in C3H10T1/2 fibroblasts during the G1 and S phases of the cell cycle. Previous studies demonstrated that the mRNA encoding CTP:phosphocholine cytidylyltransferase (CT ) increases during S phase (Golfman, L. S., Bakovic, M., and Vance, D. E. (2001) J. Biol. Chem. 276, 43688–43692) and that this activation is driven by increased binding of Sp1 to the CT promoter (Banchio, C., Schang, L. M., and Vance, D. E. (2003) J. Biol. Chem. 278, 32457–32464). We now demonstrate that cyclin-dependent kinase 2 (CDK2) phosphorylation of Sp1 activates CT transcription during S phase. Sp1 binds in a phosphorylated state to the CT promoter. Sp1 binding is enhanced by association with cyclin A/E and CDK2, both in vivo and in vitro. In cells that overexpress Sp1, co-expression of cyclin A and CDK2 induces a high and constant level of CT expression, whereas reduction in the expression of cyclin A, cyclin E, and CDK2 eliminates the induction of CT expression in S phase. Furthermore, CT expression is decreased in cells overexpressing a dominant-negative form of CDK2 and in cells treated with the CDK2 kinase inhibitors roscovitine and olomoucine. These results enhance our understanding of the regulatory mechanisms involved in the expression of CT in preparation for cell division.Fil: Banchio, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Schang, Luis M.. University of Alberta; CanadáFil: Vance, Dennis E.. University of Alberta; CanadáAmerican Society for Biochemistry and Molecular Biology2004-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/185571Banchio, Claudia Elena; Schang, Luis M.; Vance, Dennis E.; Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 38; 9-2004; 40220-402260021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.jbc.org/article/S0021-9258(20)72834-6/fulltextinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M406468200info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:54:35Zoai:ri.conicet.gov.ar:11336/185571instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:54:35.298CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
title Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
spellingShingle Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
Banchio, Claudia Elena
Phosphorylation
CTP
title_short Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
title_full Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
title_fullStr Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
title_full_unstemmed Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
title_sort Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle
dc.creator.none.fl_str_mv Banchio, Claudia Elena
Schang, Luis M.
Vance, Dennis E.
author Banchio, Claudia Elena
author_facet Banchio, Claudia Elena
Schang, Luis M.
Vance, Dennis E.
author_role author
author2 Schang, Luis M.
Vance, Dennis E.
author2_role author
author
dc.subject.none.fl_str_mv Phosphorylation
CTP
topic Phosphorylation
CTP
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Phosphatidylcholine is the major lipid component in mammalian membranes. Phosphatidylcholine synthesis increases in C3H10T1/2 fibroblasts during the G1 and S phases of the cell cycle. Previous studies demonstrated that the mRNA encoding CTP:phosphocholine cytidylyltransferase (CT ) increases during S phase (Golfman, L. S., Bakovic, M., and Vance, D. E. (2001) J. Biol. Chem. 276, 43688–43692) and that this activation is driven by increased binding of Sp1 to the CT promoter (Banchio, C., Schang, L. M., and Vance, D. E. (2003) J. Biol. Chem. 278, 32457–32464). We now demonstrate that cyclin-dependent kinase 2 (CDK2) phosphorylation of Sp1 activates CT transcription during S phase. Sp1 binds in a phosphorylated state to the CT promoter. Sp1 binding is enhanced by association with cyclin A/E and CDK2, both in vivo and in vitro. In cells that overexpress Sp1, co-expression of cyclin A and CDK2 induces a high and constant level of CT expression, whereas reduction in the expression of cyclin A, cyclin E, and CDK2 eliminates the induction of CT expression in S phase. Furthermore, CT expression is decreased in cells overexpressing a dominant-negative form of CDK2 and in cells treated with the CDK2 kinase inhibitors roscovitine and olomoucine. These results enhance our understanding of the regulatory mechanisms involved in the expression of CT in preparation for cell division.
Fil: Banchio, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Schang, Luis M.. University of Alberta; Canadá
Fil: Vance, Dennis E.. University of Alberta; Canadá
description Phosphatidylcholine is the major lipid component in mammalian membranes. Phosphatidylcholine synthesis increases in C3H10T1/2 fibroblasts during the G1 and S phases of the cell cycle. Previous studies demonstrated that the mRNA encoding CTP:phosphocholine cytidylyltransferase (CT ) increases during S phase (Golfman, L. S., Bakovic, M., and Vance, D. E. (2001) J. Biol. Chem. 276, 43688–43692) and that this activation is driven by increased binding of Sp1 to the CT promoter (Banchio, C., Schang, L. M., and Vance, D. E. (2003) J. Biol. Chem. 278, 32457–32464). We now demonstrate that cyclin-dependent kinase 2 (CDK2) phosphorylation of Sp1 activates CT transcription during S phase. Sp1 binds in a phosphorylated state to the CT promoter. Sp1 binding is enhanced by association with cyclin A/E and CDK2, both in vivo and in vitro. In cells that overexpress Sp1, co-expression of cyclin A and CDK2 induces a high and constant level of CT expression, whereas reduction in the expression of cyclin A, cyclin E, and CDK2 eliminates the induction of CT expression in S phase. Furthermore, CT expression is decreased in cells overexpressing a dominant-negative form of CDK2 and in cells treated with the CDK2 kinase inhibitors roscovitine and olomoucine. These results enhance our understanding of the regulatory mechanisms involved in the expression of CT in preparation for cell division.
publishDate 2004
dc.date.none.fl_str_mv 2004-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/185571
Banchio, Claudia Elena; Schang, Luis M.; Vance, Dennis E.; Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 38; 9-2004; 40220-40226
0021-9258
CONICET Digital
CONICET
url http://hdl.handle.net/11336/185571
identifier_str_mv Banchio, Claudia Elena; Schang, Luis M.; Vance, Dennis E.; Phosphorylation of Sp1 by Cyclin-dependent Kinase 2 Modulates the Role of Sp1 in CTP: Phosphocholine Cytidylyltransferase α Regulation during the S Phase of the Cell Cycle; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 38; 9-2004; 40220-40226
0021-9258
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.jbc.org/article/S0021-9258(20)72834-6/fulltext
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M406468200
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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