An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export

An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export

Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four–amino acid segment, whereas hGle1B...

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Main Authors: Kendirgi, Frederic, Barry, Dianne M., Griffis, Eric R., Powers, Maureen A., Wente, Susan R.
Format: Online
Language:English
Published: The Rockefeller University Press 2003
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172758/
id pubmed-2172758
recordtype oai_dc
spelling pubmed-21727582008-05-01 An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export Kendirgi, Frederic Barry, Dianne M. Griffis, Eric R. Powers, Maureen A. Wente, Susan R. Article Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four–amino acid segment, whereas hGle1B has a COOH-terminal 43–amino acid span. Only hGle1B, the more abundant isoform, localizes to the nuclear envelope (NE) and pore complex. To test whether hGle1 is a dynamic shuttling transport factor, we microinjected HeLa cells with recombinant hGle1 and conducted photobleaching studies of live HeLa cells expressing EGFP–hGle1. Both strategies show that hGle1 shuttles between the nucleus and cytoplasm. An internal 39–amino acid domain is necessary and sufficient for mediating nucleocytoplasmic transport. Using a cell-permeable peptide strategy, we document a role for hGle1 shuttling in mRNA export. An hGle1 shuttling domain (SD) peptide impairs the export of both total poly(A)+ RNA and the specific dihydrofolate reductase mRNA. Coincidentally, SD peptide–treated cells show decreased endogenous hGle1 localization at the NE and reduced nucleocytoplasmic shuttling of microinjected, recombinant hGle1. These findings pinpoint the first functional motif in hGle1 and link hGle1 to the dynamic mRNA export mechanism. The Rockefeller University Press 2003-03-31 /pmc/articles/PMC2172758/ /pubmed/12668658 http://dx.doi.org/10.1083/jcb.200211081 Text en Copyright © 2003, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Kendirgi, Frederic
Barry, Dianne M.
Griffis, Eric R.
Powers, Maureen A.
Wente, Susan R.
spellingShingle Kendirgi, Frederic
Barry, Dianne M.
Griffis, Eric R.
Powers, Maureen A.
Wente, Susan R.
An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
author_facet Kendirgi, Frederic
Barry, Dianne M.
Griffis, Eric R.
Powers, Maureen A.
Wente, Susan R.
author_sort Kendirgi, Frederic
title An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
title_short An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
title_full An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
title_fullStr An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
title_full_unstemmed An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export
title_sort essential role for hgle1 nucleocytoplasmic shuttling in mrna export
description Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four–amino acid segment, whereas hGle1B has a COOH-terminal 43–amino acid span. Only hGle1B, the more abundant isoform, localizes to the nuclear envelope (NE) and pore complex. To test whether hGle1 is a dynamic shuttling transport factor, we microinjected HeLa cells with recombinant hGle1 and conducted photobleaching studies of live HeLa cells expressing EGFP–hGle1. Both strategies show that hGle1 shuttles between the nucleus and cytoplasm. An internal 39–amino acid domain is necessary and sufficient for mediating nucleocytoplasmic transport. Using a cell-permeable peptide strategy, we document a role for hGle1 shuttling in mRNA export. An hGle1 shuttling domain (SD) peptide impairs the export of both total poly(A)+ RNA and the specific dihydrofolate reductase mRNA. Coincidentally, SD peptide–treated cells show decreased endogenous hGle1 localization at the NE and reduced nucleocytoplasmic shuttling of microinjected, recombinant hGle1. These findings pinpoint the first functional motif in hGle1 and link hGle1 to the dynamic mRNA export mechanism.
publisher The Rockefeller University Press
publishDate 2003
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172758/
_version_ 1611425040417423360

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