A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1

David M. Keller; Xiaoya Zeng; Yun Wang; Qing Hong Zhang; Mini Kapoor; Hongjun Shu; Richard Goodman; Guillermina Lozano; Yingming Zhao; Hua Lu

doi:10.1016/S1097-2765(01)00176-9

A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1

David M. Keller, Xiaoya Zeng, Yun Wang, Qing Hong Zhang, Mini Kapoor, Hongjun Shu, Richard Goodman, Guillermina Lozano, Yingming Zhao, Hua Lu

Vollum Institute

Research output: Contribution to journal › Article › peer-review

260 Scopus citations

Abstract

Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not γ irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.

Original language	English (US)
Pages (from-to)	283-292
Number of pages	10
Journal	Molecular Cell
Volume	7
Issue number	2
DOIs	https://doi.org/10.1016/S1097-2765(01)00176-9
State	Published - 2001

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/S1097-2765(01)00176-9

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@article{7ff2ed60617b403ea21dd4bea304b9fa,

title = "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1",

abstract = "Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not γ irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.",

author = "Keller, {David M.} and Xiaoya Zeng and Yun Wang and Zhang, {Qing Hong} and Mini Kapoor and Hongjun Shu and Richard Goodman and Guillermina Lozano and Yingming Zhao and Hua Lu",

note = "Funding Information: We thank Kathleen M. Alexander for helping in preparation of this manuscript and Stephen Lipard, Danny Reinberg, Nikola Pavletich, and Ze'ev Ronai for generously providing us with reagents used in this study. D. M. K. is supported by the NEI predoctoral fellowship. Q. H. Z. and R. G. are supported by NIH grants. Y. W., H. S., and Y. Z. are supported by NIH grants. This work is partly supported by grants to H. L. from NIH and ACS.",

year = "2001",

doi = "10.1016/S1097-2765(01)00176-9",

language = "English (US)",

volume = "7",

pages = "283--292",

journal = "Molecular Cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "2",

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TY - JOUR

T1 - A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1

AU - Keller, David M.

AU - Zeng, Xiaoya

AU - Wang, Yun

AU - Zhang, Qing Hong

AU - Kapoor, Mini

AU - Shu, Hongjun

AU - Goodman, Richard

AU - Lozano, Guillermina

AU - Zhao, Yingming

AU - Lu, Hua

N1 - Funding Information: We thank Kathleen M. Alexander for helping in preparation of this manuscript and Stephen Lipard, Danny Reinberg, Nikola Pavletich, and Ze'ev Ronai for generously providing us with reagents used in this study. D. M. K. is supported by the NEI predoctoral fellowship. Q. H. Z. and R. G. are supported by NIH grants. Y. W., H. S., and Y. Z. are supported by NIH grants. This work is partly supported by grants to H. L. from NIH and ACS.

PY - 2001

Y1 - 2001

N2 - Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not γ irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.

AB - Phosphorylation of the human p53 protein at Ser-392 has been shown to be responsive to UV but not γ irradiation. Here we describe identification and purification of a mammalian UV-activated protein kinase complex that phosphorylates Ser-392 of p53 in vitro. This kinase complex contains casein kinase 2 (CK2) and the chromatin transcriptional elongation factor FACT (a heterodimer of hSpt16 and SSRP1). In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53 over other substrates including casein. In addition, phosphorylation by the kinase complex enhances p53 activity. These results thus provide a potential mechanism for p53 activation by UV irradiation.

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AN - SCOPUS:17744384255

SN - 1097-2765

VL - 7

SP - 283

EP - 292

JO - Molecular Cell

JF - Molecular Cell

IS - 2

ER -

A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1

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