PITSLRE p110 protein kinases associate with transcription complexes and affect their activity

Janeen H. Trembley, Dongli Hu, Li Chung Hsu, Cho Yau Yeung, Clive A. Slaughter, Jill M. Lahti, Vincent J. Kidd

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

Although the PITSLRE protein kinases are members of the cyclin-dependent kinase superfamily, their cellular function is unclear. Previously we demonstrated that the general RNA splicing factor RNPS1 is a specific PITSLRE p110 kinase interactor in vivo. This suggests that the PITSLRE family of protein kinases is involved in some aspect of RNA processing or transcription. Here we identify multiple transcriptional elongation factors, including ELL2, TFIIF1, TFIIS, and FACT, as PITSLRE kinase-associated proteins. We demonstrate that PITSLRE p110 protein kinases co-immunoprecipitate and/or co-purify with these elongation factors as well as with RNA polymerase II. Antibody-mediated inhibition of PITSLRE kinase specifically suppressed RNA polymerase II-dependent in vitro transcription initiated at a GC-rich (adenosine deaminase) or TATA box-dependent (Ad2ML) promoter, and this suppression was rescued by readdition of purified PITSLRE p110 kinase. Together, these data strongly suggest that PITSLRE protein kinases participate in a signaling pathway that potentially regulates or links transcription and RNA processing events.

Original languageEnglish (US)
Pages (from-to)2589-2596
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number4
DOIs
StatePublished - Jan 25 2002
Externally publishedYes

Fingerprint

Transcription
Protein Kinases
Phosphotransferases
RNA Polymerase II
RNA
Transcriptional Elongation Factors
Peptide Elongation Factors
TATA Box
Adenosine Deaminase
Cyclin-Dependent Kinases
Processing
Antibodies
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

PITSLRE p110 protein kinases associate with transcription complexes and affect their activity. / Trembley, Janeen H.; Hu, Dongli; Hsu, Li Chung; Yeung, Cho Yau; Slaughter, Clive A.; Lahti, Jill M.; Kidd, Vincent J.

In: Journal of Biological Chemistry, Vol. 277, No. 4, 25.01.2002, p. 2589-2596.

Research output: Contribution to journalArticle

Trembley, Janeen H. ; Hu, Dongli ; Hsu, Li Chung ; Yeung, Cho Yau ; Slaughter, Clive A. ; Lahti, Jill M. ; Kidd, Vincent J. / PITSLRE p110 protein kinases associate with transcription complexes and affect their activity. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 4. pp. 2589-2596.
@article{a4de0ee982e644b5835e0960baafea7e,
title = "PITSLRE p110 protein kinases associate with transcription complexes and affect their activity",
abstract = "Although the PITSLRE protein kinases are members of the cyclin-dependent kinase superfamily, their cellular function is unclear. Previously we demonstrated that the general RNA splicing factor RNPS1 is a specific PITSLRE p110 kinase interactor in vivo. This suggests that the PITSLRE family of protein kinases is involved in some aspect of RNA processing or transcription. Here we identify multiple transcriptional elongation factors, including ELL2, TFIIF1, TFIIS, and FACT, as PITSLRE kinase-associated proteins. We demonstrate that PITSLRE p110 protein kinases co-immunoprecipitate and/or co-purify with these elongation factors as well as with RNA polymerase II. Antibody-mediated inhibition of PITSLRE kinase specifically suppressed RNA polymerase II-dependent in vitro transcription initiated at a GC-rich (adenosine deaminase) or TATA box-dependent (Ad2ML) promoter, and this suppression was rescued by readdition of purified PITSLRE p110 kinase. Together, these data strongly suggest that PITSLRE protein kinases participate in a signaling pathway that potentially regulates or links transcription and RNA processing events.",
author = "Trembley, {Janeen H.} and Dongli Hu and Hsu, {Li Chung} and Yeung, {Cho Yau} and Slaughter, {Clive A.} and Lahti, {Jill M.} and Kidd, {Vincent J.}",
year = "2002",
month = "1",
day = "25",
doi = "10.1074/jbc.M109755200",
language = "English (US)",
volume = "277",
pages = "2589--2596",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "4",

}

TY - JOUR

T1 - PITSLRE p110 protein kinases associate with transcription complexes and affect their activity

AU - Trembley, Janeen H.

AU - Hu, Dongli

AU - Hsu, Li Chung

AU - Yeung, Cho Yau

AU - Slaughter, Clive A.

AU - Lahti, Jill M.

AU - Kidd, Vincent J.

PY - 2002/1/25

Y1 - 2002/1/25

N2 - Although the PITSLRE protein kinases are members of the cyclin-dependent kinase superfamily, their cellular function is unclear. Previously we demonstrated that the general RNA splicing factor RNPS1 is a specific PITSLRE p110 kinase interactor in vivo. This suggests that the PITSLRE family of protein kinases is involved in some aspect of RNA processing or transcription. Here we identify multiple transcriptional elongation factors, including ELL2, TFIIF1, TFIIS, and FACT, as PITSLRE kinase-associated proteins. We demonstrate that PITSLRE p110 protein kinases co-immunoprecipitate and/or co-purify with these elongation factors as well as with RNA polymerase II. Antibody-mediated inhibition of PITSLRE kinase specifically suppressed RNA polymerase II-dependent in vitro transcription initiated at a GC-rich (adenosine deaminase) or TATA box-dependent (Ad2ML) promoter, and this suppression was rescued by readdition of purified PITSLRE p110 kinase. Together, these data strongly suggest that PITSLRE protein kinases participate in a signaling pathway that potentially regulates or links transcription and RNA processing events.

AB - Although the PITSLRE protein kinases are members of the cyclin-dependent kinase superfamily, their cellular function is unclear. Previously we demonstrated that the general RNA splicing factor RNPS1 is a specific PITSLRE p110 kinase interactor in vivo. This suggests that the PITSLRE family of protein kinases is involved in some aspect of RNA processing or transcription. Here we identify multiple transcriptional elongation factors, including ELL2, TFIIF1, TFIIS, and FACT, as PITSLRE kinase-associated proteins. We demonstrate that PITSLRE p110 protein kinases co-immunoprecipitate and/or co-purify with these elongation factors as well as with RNA polymerase II. Antibody-mediated inhibition of PITSLRE kinase specifically suppressed RNA polymerase II-dependent in vitro transcription initiated at a GC-rich (adenosine deaminase) or TATA box-dependent (Ad2ML) promoter, and this suppression was rescued by readdition of purified PITSLRE p110 kinase. Together, these data strongly suggest that PITSLRE protein kinases participate in a signaling pathway that potentially regulates or links transcription and RNA processing events.

UR - http://www.scopus.com/inward/record.url?scp=0037169530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037169530&partnerID=8YFLogxK

U2 - 10.1074/jbc.M109755200

DO - 10.1074/jbc.M109755200

M3 - Article

VL - 277

SP - 2589

EP - 2596

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 4

ER -