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PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains.

Standard

PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. / Möller, Andreas; Sirma, Hüseyin; Hofmann, Thomas G; Rueffer, Sven; Klimczak, Elisabeth; Dröge, Wulf; Will, Hans; Schmitz, M Lienhard.

in: CANCER RES, Jahrgang 63, Nr. 15, 15, 2003, S. 4310-4314.

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

Harvard

Möller, A, Sirma, H, Hofmann, TG, Rueffer, S, Klimczak, E, Dröge, W, Will, H & Schmitz, ML 2003, 'PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains.', CANCER RES, Jg. 63, Nr. 15, 15, S. 4310-4314. <http://www.ncbi.nlm.nih.gov/pubmed/12907596?dopt=Citation>

APA

Möller, A., Sirma, H., Hofmann, T. G., Rueffer, S., Klimczak, E., Dröge, W., Will, H., & Schmitz, M. L. (2003). PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. CANCER RES, 63(15), 4310-4314. [15]. http://www.ncbi.nlm.nih.gov/pubmed/12907596?dopt=Citation

Vancouver

Möller A, Sirma H, Hofmann TG, Rueffer S, Klimczak E, Dröge W et al. PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. CANCER RES. 2003;63(15):4310-4314. 15.

Bibtex

@article{6ea6932c080a46c293739968ef1aa5c5,
title = "PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains.",
abstract = "Here we demonstrate that endogenous human homeodomain-interacting protein kinase (HIPK) 2 and the highly homologous kinase HIPK3 are found in a novel subnuclear domain, the HIPK domains. These are distinct from other subnuclear structures such as Cajal bodies and nucleoli and show only a partial colocalization with promyelocytic leukemia (PML) nuclear bodies (PML-NBs). A kinase inactive HIPK2 point mutant is localized in the nucleoplasm. The occurrence of HIPK domains in PML-/- fibroblasts reveals their independence from the PML protein. HIPK2 can be almost completely recruited to PML-NBs by the PML isoform PML IV, but not by PML-III. PML IV-mediated recruitment of HIPK2 does not rely on its kinase function and also occurs in PML-/- fibroblasts, showing that this PML isoform is sufficient for recruitment of HIPK2. Whereas the architecture of HIPK domains is PML independent, HIPK2-mediated enhancement of p53-dependent transcription, p53 serine 46 phosphorylation and the antiproliferative function of HIPK2 strictly rely on the presence of PML.",
author = "Andreas M{\"o}ller and H{\"u}seyin Sirma and Hofmann, {Thomas G} and Sven Rueffer and Elisabeth Klimczak and Wulf Dr{\"o}ge and Hans Will and Schmitz, {M Lienhard}",
year = "2003",
language = "Deutsch",
volume = "63",
pages = "4310--4314",
journal = "CANCER RES",
issn = "0008-5472",
publisher = "American Association for Cancer Research Inc.",
number = "15",

}

RIS

TY - JOUR

T1 - PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains.

AU - Möller, Andreas

AU - Sirma, Hüseyin

AU - Hofmann, Thomas G

AU - Rueffer, Sven

AU - Klimczak, Elisabeth

AU - Dröge, Wulf

AU - Will, Hans

AU - Schmitz, M Lienhard

PY - 2003

Y1 - 2003

N2 - Here we demonstrate that endogenous human homeodomain-interacting protein kinase (HIPK) 2 and the highly homologous kinase HIPK3 are found in a novel subnuclear domain, the HIPK domains. These are distinct from other subnuclear structures such as Cajal bodies and nucleoli and show only a partial colocalization with promyelocytic leukemia (PML) nuclear bodies (PML-NBs). A kinase inactive HIPK2 point mutant is localized in the nucleoplasm. The occurrence of HIPK domains in PML-/- fibroblasts reveals their independence from the PML protein. HIPK2 can be almost completely recruited to PML-NBs by the PML isoform PML IV, but not by PML-III. PML IV-mediated recruitment of HIPK2 does not rely on its kinase function and also occurs in PML-/- fibroblasts, showing that this PML isoform is sufficient for recruitment of HIPK2. Whereas the architecture of HIPK domains is PML independent, HIPK2-mediated enhancement of p53-dependent transcription, p53 serine 46 phosphorylation and the antiproliferative function of HIPK2 strictly rely on the presence of PML.

AB - Here we demonstrate that endogenous human homeodomain-interacting protein kinase (HIPK) 2 and the highly homologous kinase HIPK3 are found in a novel subnuclear domain, the HIPK domains. These are distinct from other subnuclear structures such as Cajal bodies and nucleoli and show only a partial colocalization with promyelocytic leukemia (PML) nuclear bodies (PML-NBs). A kinase inactive HIPK2 point mutant is localized in the nucleoplasm. The occurrence of HIPK domains in PML-/- fibroblasts reveals their independence from the PML protein. HIPK2 can be almost completely recruited to PML-NBs by the PML isoform PML IV, but not by PML-III. PML IV-mediated recruitment of HIPK2 does not rely on its kinase function and also occurs in PML-/- fibroblasts, showing that this PML isoform is sufficient for recruitment of HIPK2. Whereas the architecture of HIPK domains is PML independent, HIPK2-mediated enhancement of p53-dependent transcription, p53 serine 46 phosphorylation and the antiproliferative function of HIPK2 strictly rely on the presence of PML.

M3 - SCORING: Zeitschriftenaufsatz

VL - 63

SP - 4310

EP - 4314

JO - CANCER RES

JF - CANCER RES

SN - 0008-5472

IS - 15

M1 - 15

ER -