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Title: Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome

Abstract

TREX-2 is a five protein complex, conserved from yeast to humans, involved in linking mRNA transcription and export. The centrin 2 subunit of TREX-2 is also a component of the centrosome and is additionally involved in a distinctly different process of nuclear protein export. While centrin 2 is a known multifunctional protein, the roles of other human TREX-2 complex proteins other than mRNA export are not known. In this study, we found that human TREX-2 member PCID2 but not ENY2 is involved in some of the same cellular processes as those of centrin 2 apart from the classical TREX-2 function. PCID2 is present at the centrosome in a subset of HeLa cells and this localization is centrin 2 dependent. Furthermore, the presence of PCID2 at the centrosome is prevalent throughout the cell cycle as determined by co-staining with cyclins E, A and B. PCID2 but not ENY2 is also involved in protein export. Surprisingly, siRNA knockdown of PCID2 delayed the rate of nuclear protein export, a mechanism distinct from the effects of centrin 2, which when knocked down inhibits export. Finally we showed that co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export, indicatingmore » the dominance of the centrin 2 phenotype. Together these results represent the first discovery of specific novel functions for PCID2 other than mRNA export and suggest that components of the TREX-2 complex serve alternative shared roles in the regulation of nuclear transport and cell cycle progression. - Highlights: • TREX2 complex member PCID2 but not ENY2 localizes to the centrosome in HeLa cells. • Centrin 2 is required for the localization of PCID2 at the centrosome. • PCID2 is found at the centrosome in G1/S at a slightly higher rate than that in G2/M. • PCID2 but not ENY2 delays the rate of nuclear protein export. • Co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export.« less

Authors:
; ;  [1];  [2]
  1. Westminster College, Department of Biology, 319 South Market Street, New Wilmington, PA 16172 (United States)
  2. Section of Cell and Developmental Biology, Division of Biological Sciences, University of California – San Diego, 9500 Gilman Drive, 0347, La Jolla, CA 92093-0347 (United States)
Publication Date:
OSTI Identifier:
22278247
Resource Type:
Journal Article
Journal Name:
Experimental Cell Research
Additional Journal Information:
Journal Volume: 320; Journal Issue: 2; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CELL CYCLE; HELA CELLS; MESSENGER-RNA; PHENOTYPE; PROTEINS; YEASTS

Citation Formats

Cunningham, Corey N., Schmidt, Casey A., Schramm, Nathaniel J., Gaylord, Michelle R., and Resendes, Karen K., E-mail: resendkk@westminster.edu. Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome. United States: N. p., 2014. Web. doi:10.1016/J.YEXCR.2013.11.015.
Cunningham, Corey N., Schmidt, Casey A., Schramm, Nathaniel J., Gaylord, Michelle R., & Resendes, Karen K., E-mail: resendkk@westminster.edu. Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome. United States. https://doi.org/10.1016/J.YEXCR.2013.11.015
Cunningham, Corey N., Schmidt, Casey A., Schramm, Nathaniel J., Gaylord, Michelle R., and Resendes, Karen K., E-mail: resendkk@westminster.edu. 2014. "Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome". United States. https://doi.org/10.1016/J.YEXCR.2013.11.015.
@article{osti_22278247,
title = {Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome},
author = {Cunningham, Corey N. and Schmidt, Casey A. and Schramm, Nathaniel J. and Gaylord, Michelle R. and Resendes, Karen K., E-mail: resendkk@westminster.edu},
abstractNote = {TREX-2 is a five protein complex, conserved from yeast to humans, involved in linking mRNA transcription and export. The centrin 2 subunit of TREX-2 is also a component of the centrosome and is additionally involved in a distinctly different process of nuclear protein export. While centrin 2 is a known multifunctional protein, the roles of other human TREX-2 complex proteins other than mRNA export are not known. In this study, we found that human TREX-2 member PCID2 but not ENY2 is involved in some of the same cellular processes as those of centrin 2 apart from the classical TREX-2 function. PCID2 is present at the centrosome in a subset of HeLa cells and this localization is centrin 2 dependent. Furthermore, the presence of PCID2 at the centrosome is prevalent throughout the cell cycle as determined by co-staining with cyclins E, A and B. PCID2 but not ENY2 is also involved in protein export. Surprisingly, siRNA knockdown of PCID2 delayed the rate of nuclear protein export, a mechanism distinct from the effects of centrin 2, which when knocked down inhibits export. Finally we showed that co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export, indicating the dominance of the centrin 2 phenotype. Together these results represent the first discovery of specific novel functions for PCID2 other than mRNA export and suggest that components of the TREX-2 complex serve alternative shared roles in the regulation of nuclear transport and cell cycle progression. - Highlights: • TREX2 complex member PCID2 but not ENY2 localizes to the centrosome in HeLa cells. • Centrin 2 is required for the localization of PCID2 at the centrosome. • PCID2 is found at the centrosome in G1/S at a slightly higher rate than that in G2/M. • PCID2 but not ENY2 delays the rate of nuclear protein export. • Co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export.},
doi = {10.1016/J.YEXCR.2013.11.015},
url = {https://www.osti.gov/biblio/22278247}, journal = {Experimental Cell Research},
issn = {0014-4827},
number = 2,
volume = 320,
place = {United States},
year = {Wed Jan 15 00:00:00 EST 2014},
month = {Wed Jan 15 00:00:00 EST 2014}
}