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Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2.

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Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. / Hofmann, Thomas G; Möller, Andreas; Sirma, Hüseyin; Zentgraf, Hanswalter; Taya, Yoichi; Dröge, Wulf; Will, Hans; Schmitz, M Lienhard.

in: NAT CELL BIOL, Jahrgang 4, Nr. 1, 1, 2002, S. 1-10.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Hofmann, TG, Möller, A, Sirma, H, Zentgraf, H, Taya, Y, Dröge, W, Will, H & Schmitz, ML 2002, 'Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2.', NAT CELL BIOL, Jg. 4, Nr. 1, 1, S. 1-10. <http://www.ncbi.nlm.nih.gov/pubmed/11740489?dopt=Citation>

APA

Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L. (2002). Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. NAT CELL BIOL, 4(1), 1-10. [1]. http://www.ncbi.nlm.nih.gov/pubmed/11740489?dopt=Citation

Vancouver

Hofmann TG, Möller A, Sirma H, Zentgraf H, Taya Y, Dröge W et al. Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2. NAT CELL BIOL. 2002;4(1):1-10. 1.

Bibtex

@article{8f66805f138b45ee9e685c0ceafc4670,
title = "Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2.",
abstract = "Transcriptional activity of p53, a central regulatory switch in a network controlling cell proliferation and apoptosis, is modulated by protein stability and post-translational modifications including phosphorylation and acetylation. Here we demonstrate that the human serine/threonine kinase homeodomain-interacting protein kinase-2 (HIPK2) colocalizes and interacts with p53 and CREB-binding protein (CBP) within promyelocytic leukaemia (PML) nuclear bodies. HIPK2 is activated by ultraviolet (UV) radiation and selectively phosphorylates p53 at Ser 46, thus facilitating the CBP-mediated acetylation of p53 at Lys 382, and promoting p53-dependent gene expression. Accordingly, the kinase function of HIPK2 mediates the increased expression of p53 target genes, which results in growth arrest and the enhancement of UV-induced apoptosis. Interference with HIPK2 expression by antisense oligonucleotides impairs UV-induced apoptosis. Our results imply that HIPK2 is a novel regulator of p53 effector functions involved in cell growth, proliferation and apoptosis.",
author = "Hofmann, {Thomas G} and Andreas M{\"o}ller and H{\"u}seyin Sirma and Hanswalter Zentgraf and Yoichi Taya and Wulf Dr{\"o}ge and Hans Will and Schmitz, {M Lienhard}",
year = "2002",
language = "Deutsch",
volume = "4",
pages = "1--10",
journal = "NAT CELL BIOL",
issn = "1465-7392",
publisher = "NATURE PUBLISHING GROUP",
number = "1",

}

RIS

TY - JOUR

T1 - Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2.

AU - Hofmann, Thomas G

AU - Möller, Andreas

AU - Sirma, Hüseyin

AU - Zentgraf, Hanswalter

AU - Taya, Yoichi

AU - Dröge, Wulf

AU - Will, Hans

AU - Schmitz, M Lienhard

PY - 2002

Y1 - 2002

N2 - Transcriptional activity of p53, a central regulatory switch in a network controlling cell proliferation and apoptosis, is modulated by protein stability and post-translational modifications including phosphorylation and acetylation. Here we demonstrate that the human serine/threonine kinase homeodomain-interacting protein kinase-2 (HIPK2) colocalizes and interacts with p53 and CREB-binding protein (CBP) within promyelocytic leukaemia (PML) nuclear bodies. HIPK2 is activated by ultraviolet (UV) radiation and selectively phosphorylates p53 at Ser 46, thus facilitating the CBP-mediated acetylation of p53 at Lys 382, and promoting p53-dependent gene expression. Accordingly, the kinase function of HIPK2 mediates the increased expression of p53 target genes, which results in growth arrest and the enhancement of UV-induced apoptosis. Interference with HIPK2 expression by antisense oligonucleotides impairs UV-induced apoptosis. Our results imply that HIPK2 is a novel regulator of p53 effector functions involved in cell growth, proliferation and apoptosis.

AB - Transcriptional activity of p53, a central regulatory switch in a network controlling cell proliferation and apoptosis, is modulated by protein stability and post-translational modifications including phosphorylation and acetylation. Here we demonstrate that the human serine/threonine kinase homeodomain-interacting protein kinase-2 (HIPK2) colocalizes and interacts with p53 and CREB-binding protein (CBP) within promyelocytic leukaemia (PML) nuclear bodies. HIPK2 is activated by ultraviolet (UV) radiation and selectively phosphorylates p53 at Ser 46, thus facilitating the CBP-mediated acetylation of p53 at Lys 382, and promoting p53-dependent gene expression. Accordingly, the kinase function of HIPK2 mediates the increased expression of p53 target genes, which results in growth arrest and the enhancement of UV-induced apoptosis. Interference with HIPK2 expression by antisense oligonucleotides impairs UV-induced apoptosis. Our results imply that HIPK2 is a novel regulator of p53 effector functions involved in cell growth, proliferation and apoptosis.

M3 - SCORING: Zeitschriftenaufsatz

VL - 4

SP - 1

EP - 10

JO - NAT CELL BIOL

JF - NAT CELL BIOL

SN - 1465-7392

IS - 1

M1 - 1

ER -