FEBS Letters, volume 593, issue 10, pages 1102-1112
Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila
Kachaev Zaur M
1
,
Lebedeva Lyubov
1
,
Shaposhnikov Alexander V.
1
,
Moresco J. J.
2
,
Yates John T.
2
,
Schedl Paul D
1, 3
,
Shidlovskii Y. V.
1, 4
2
Department of Chemical Physiology The Scripps Research Institute La Jolla CA USA
|
3
Department of Molecular Biology Princeton University Princeton NJ USA
|
Publication type: Journal Article
Publication date: 2019-04-29
Journal:
FEBS Letters
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 3.5
ISSN: 00145793, 18733468
PubMed ID:
31001806
Biochemistry
Molecular Biology
Cell Biology
Genetics
Structural Biology
Biophysics
Abstract
The Paip2 protein is a factor regulating mRNA translation and stability in the cytoplasm. It has also been found in the nuclei of several cell types in Drosophila. Here, we aim to elucidate the functions of Paip2 in the cell nucleus. We find that nuclear Paip2 is a component of an ~300‐kDa protein complex. Paip2 interacts with mRNA capping factor and factors of RNA polymerase II (Pol II) transcription initiation and early elongation. Paip2 functionally cooperates with the Cbp80 subunit of the cap‐binding complex, with both proteins ensuring proper Pol II C‐terminal domain (CTD) Ser5 phosphorylation at the promoter. Thus, Paip2 is a novel player at the stage of mRNA capping and early Pol II elongation.
Citations by journals
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Bioscience Reports
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1 publication, 16.67%
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1 publication, 16.67%
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1 publication, 16.67%
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Life Science Alliance
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1 publication, 16.67%
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Genes and Development
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1 publication, 16.67%
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Cold Spring Harbor Symposia on Quantitative Biology
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1 publication, 16.67%
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1
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Citations by publishers
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1
2
3
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Cold Spring Harbor Laboratory
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Cold Spring Harbor Laboratory
3 publications, 50%
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Springer Nature
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Springer Nature
1 publication, 16.67%
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
1 publication, 16.67%
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Rockefeller University Press
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Rockefeller University Press
1 publication, 16.67%
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1
2
3
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Kachaev Z. M. et al. Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila // FEBS Letters. 2019. Vol. 593. No. 10. pp. 1102-1112.
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Kachaev Z. M., Lebedeva L., Shaposhnikov A. V., Moresco J. J., Yates J. T., Schedl P. D., Shidlovskii Y. V. Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila // FEBS Letters. 2019. Vol. 593. No. 10. pp. 1102-1112.
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TY - JOUR
DO - 10.1002/1873-3468.13391
UR - https://doi.org/10.1002%2F1873-3468.13391
TI - Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila
T2 - FEBS Letters
AU - Shaposhnikov, Alexander V.
AU - Shidlovskii, Y. V.
AU - Kachaev, Zaur M
AU - Lebedeva, Lyubov
AU - Moresco, J. J.
AU - Yates, John T.
AU - Schedl, Paul D
PY - 2019
DA - 2019/04/29 00:00:00
PB - Wiley
SP - 1102-1112
IS - 10
VL - 593
PMID - 31001806
SN - 0014-5793
SN - 1873-3468
ER -
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@article{2019_Kachaev,
author = {Alexander V. Shaposhnikov and Y. V. Shidlovskii and Zaur M Kachaev and Lyubov Lebedeva and J. J. Moresco and John T. Yates and Paul D Schedl},
title = {Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila},
journal = {FEBS Letters},
year = {2019},
volume = {593},
publisher = {Wiley},
month = {apr},
url = {https://doi.org/10.1002%2F1873-3468.13391},
number = {10},
pages = {1102--1112},
doi = {10.1002/1873-3468.13391}
}
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MLA
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Kachaev, Zaur M., et al. “Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.” FEBS Letters, vol. 593, no. 10, Apr. 2019, pp. 1102-1112. https://doi.org/10.1002%2F1873-3468.13391.
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