Protein kinase C phosphorylates DNA topoisomerase I

D. Scott Samuels; Yoshiko Shimizu; Nobuyoshi Shimizi

doi:10.1016/0014-5793(89)81493-0

Protein kinase C phosphorylates DNA topoisomerase I

D. Scott Samuels, Yoshiko Shimizu, Nobuyoshi Shimizi

Division of Biological and Biomedical Sciences

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

62 Scopus citations

Abstract

The induction of mammalian cell proliferation requires the expression of a specific set of genes. Tumor promoters stimulate cell growth by activating the Ca²⁺ and phospholipid-dependent protein kinase, protein kinase C (PKC). DNA topoisomerase I, a nuclear enzyme involved in transcription, was phosphorylated by activated PKC in vitro. Phosphorylation by PKC stimulated the DNA relaxation activity of topoisomerase I two- to three-fold. Therefore, DNA topoisomerase I is a substrate for PKC-mediated activation by phosphorylation and may serve as a nuclear target of mitogenic signals generated by tumor promoters in vivo.

Original language	English
Pages (from-to)	57-60
Number of pages	4
Journal	FEBS Letters
Volume	259
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(89)81493-0
State	Published - Dec 18 1989

Keywords

Mitogenic signal transduction
Nuclear target
Protein kinase C
Protein phosphorylation
Topoisomerase I, DNA-

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title = "Protein kinase C phosphorylates DNA topoisomerase I",

abstract = "The induction of mammalian cell proliferation requires the expression of a specific set of genes. Tumor promoters stimulate cell growth by activating the Ca2+ and phospholipid-dependent protein kinase, protein kinase C (PKC). DNA topoisomerase I, a nuclear enzyme involved in transcription, was phosphorylated by activated PKC in vitro. Phosphorylation by PKC stimulated the DNA relaxation activity of topoisomerase I two- to three-fold. Therefore, DNA topoisomerase I is a substrate for PKC-mediated activation by phosphorylation and may serve as a nuclear target of mitogenic signals generated by tumor promoters in vivo.",

keywords = "Mitogenic signal transduction, Nuclear target, Protein kinase C, Protein phosphorylation, Topoisomerase I, DNA-",

author = "Samuels, \{D. Scott\} and Yoshiko Shimizu and Nobuyoshi Shimizi",

note = "Funding Information: AcknowledgementTsh: is work wass upportedb y a Public HealthS er-vice grant from the National Instituteso f Health (GM-24375a) nd a predoctoratl raininga wards ponsoredb y a NationalR esearchS ervice Award from the NationalC ancerI nstitute( CA-09213)W. e thankD r Grace Pavlath for criticalr eadingo f the manuscripta nd Dr Samuel Ward for technicala dviceo n immunoprecipitation.",

year = "1989",

month = dec,

day = "18",

doi = "10.1016/0014-5793(89)81493-0",

language = "English",

volume = "259",

pages = "57--60",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

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TY - JOUR

T1 - Protein kinase C phosphorylates DNA topoisomerase I

AU - Samuels, D. Scott

AU - Shimizu, Yoshiko

AU - Shimizi, Nobuyoshi

N1 - Funding Information: AcknowledgementTsh: is work wass upportedb y a Public HealthS er-vice grant from the National Instituteso f Health (GM-24375a) nd a predoctoratl raininga wards ponsoredb y a NationalR esearchS ervice Award from the NationalC ancerI nstitute( CA-09213)W. e thankD r Grace Pavlath for criticalr eadingo f the manuscripta nd Dr Samuel Ward for technicala dviceo n immunoprecipitation.

PY - 1989/12/18

Y1 - 1989/12/18

N2 - The induction of mammalian cell proliferation requires the expression of a specific set of genes. Tumor promoters stimulate cell growth by activating the Ca2+ and phospholipid-dependent protein kinase, protein kinase C (PKC). DNA topoisomerase I, a nuclear enzyme involved in transcription, was phosphorylated by activated PKC in vitro. Phosphorylation by PKC stimulated the DNA relaxation activity of topoisomerase I two- to three-fold. Therefore, DNA topoisomerase I is a substrate for PKC-mediated activation by phosphorylation and may serve as a nuclear target of mitogenic signals generated by tumor promoters in vivo.

AB - The induction of mammalian cell proliferation requires the expression of a specific set of genes. Tumor promoters stimulate cell growth by activating the Ca2+ and phospholipid-dependent protein kinase, protein kinase C (PKC). DNA topoisomerase I, a nuclear enzyme involved in transcription, was phosphorylated by activated PKC in vitro. Phosphorylation by PKC stimulated the DNA relaxation activity of topoisomerase I two- to three-fold. Therefore, DNA topoisomerase I is a substrate for PKC-mediated activation by phosphorylation and may serve as a nuclear target of mitogenic signals generated by tumor promoters in vivo.

KW - Mitogenic signal transduction

KW - Nuclear target

KW - Protein kinase C

KW - Protein phosphorylation

KW - Topoisomerase I, DNA-

UR - https://www.scopus.com/pages/publications/0024804104

U2 - 10.1016/0014-5793(89)81493-0

DO - 10.1016/0014-5793(89)81493-0

M3 - Article

C2 - 2557245

AN - SCOPUS:0024804104

SN - 0014-5793

VL - 259

SP - 57

EP - 60

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Protein kinase C phosphorylates DNA topoisomerase I

Abstract

Keywords

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