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Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression.

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Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. / Möller, Andreas; Sirma, Hüseyin; Hofmann, Thomas G; Staege, Hannah; Gresko, Ekaterina; Schmid, Lüdi Katharina; Klimczak, Elisabeth; Dröge, Wulf; Will, Hans; Schmitz, M Lienhard.

in: ONCOGENE, Jahrgang 22, Nr. 54, 54, 2003, S. 8731-8737.

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

Harvard

Möller, A, Sirma, H, Hofmann, TG, Staege, H, Gresko, E, Schmid, LK, Klimczak, E, Dröge, W, Will, H & Schmitz, ML 2003, 'Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression.', ONCOGENE, Jg. 22, Nr. 54, 54, S. 8731-8737. <http://www.ncbi.nlm.nih.gov/pubmed/14647468?dopt=Citation>

APA

Möller, A., Sirma, H., Hofmann, T. G., Staege, H., Gresko, E., Schmid, L. K., Klimczak, E., Dröge, W., Will, H., & Schmitz, M. L. (2003). Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. ONCOGENE, 22(54), 8731-8737. [54]. http://www.ncbi.nlm.nih.gov/pubmed/14647468?dopt=Citation

Vancouver

Möller A, Sirma H, Hofmann TG, Staege H, Gresko E, Schmid LK et al. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. ONCOGENE. 2003;22(54):8731-8737. 54.

Bibtex

@article{b0a0586492c34b9aa7255626cbf1632c,
title = "Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression.",
abstract = "HIPK2 shows overlapping localization with p53 in promyelocytic leukemia (PML) nuclear bodies (PML-NBs) and functionally interacts with p53 to increase gene expression. Here we demonstrate that HIPK2 and the PML-NB resident protein Sp100 synergize for the activation of p53-dependent gene expression. Sp100 and HIPK2 interact and partially colocalize in PML-NBs. The cooperation of HIPK2 and Sp100 for the induction of p21(Waf1) is completely dependent on the presence of p53 and the kinase function of HIPK2. Downregulation of Sp100 levels by expression of siRNA does not interfere with p53-mediated transcription, but obviates the enhancing effect of HIPK2. In summary, these experiments reveal a novel function for Sp100 as a coactivator for HIPK2-mediated p53 activation.",
author = "Andreas M{\"o}ller and H{\"u}seyin Sirma and Hofmann, {Thomas G} and Hannah Staege and Ekaterina Gresko and Schmid, {L{\"u}di Katharina} and Elisabeth Klimczak and Wulf Dr{\"o}ge and Hans Will and Schmitz, {M Lienhard}",
year = "2003",
language = "Deutsch",
volume = "22",
pages = "8731--8737",
journal = "ONCOGENE",
issn = "0950-9232",
publisher = "NATURE PUBLISHING GROUP",
number = "54",

}

RIS

TY - JOUR

T1 - Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression.

AU - Möller, Andreas

AU - Sirma, Hüseyin

AU - Hofmann, Thomas G

AU - Staege, Hannah

AU - Gresko, Ekaterina

AU - Schmid, Lüdi Katharina

AU - Klimczak, Elisabeth

AU - Dröge, Wulf

AU - Will, Hans

AU - Schmitz, M Lienhard

PY - 2003

Y1 - 2003

N2 - HIPK2 shows overlapping localization with p53 in promyelocytic leukemia (PML) nuclear bodies (PML-NBs) and functionally interacts with p53 to increase gene expression. Here we demonstrate that HIPK2 and the PML-NB resident protein Sp100 synergize for the activation of p53-dependent gene expression. Sp100 and HIPK2 interact and partially colocalize in PML-NBs. The cooperation of HIPK2 and Sp100 for the induction of p21(Waf1) is completely dependent on the presence of p53 and the kinase function of HIPK2. Downregulation of Sp100 levels by expression of siRNA does not interfere with p53-mediated transcription, but obviates the enhancing effect of HIPK2. In summary, these experiments reveal a novel function for Sp100 as a coactivator for HIPK2-mediated p53 activation.

AB - HIPK2 shows overlapping localization with p53 in promyelocytic leukemia (PML) nuclear bodies (PML-NBs) and functionally interacts with p53 to increase gene expression. Here we demonstrate that HIPK2 and the PML-NB resident protein Sp100 synergize for the activation of p53-dependent gene expression. Sp100 and HIPK2 interact and partially colocalize in PML-NBs. The cooperation of HIPK2 and Sp100 for the induction of p21(Waf1) is completely dependent on the presence of p53 and the kinase function of HIPK2. Downregulation of Sp100 levels by expression of siRNA does not interfere with p53-mediated transcription, but obviates the enhancing effect of HIPK2. In summary, these experiments reveal a novel function for Sp100 as a coactivator for HIPK2-mediated p53 activation.

M3 - SCORING: Zeitschriftenaufsatz

VL - 22

SP - 8731

EP - 8737

JO - ONCOGENE

JF - ONCOGENE

SN - 0950-9232

IS - 54

M1 - 54

ER -