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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/185571
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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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1844613657033441280 |
score |
13.070432 |