Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes

The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained unclear how Tap activity is regulated in vivo...

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Prif Awduron: Wiegand, Heather L., Coburn, Glen A., Zeng, Yan, Kang, Yibin, Bogerd, Hal P., Cullen, Bryan R.
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Cyhoeddwyd: American Society for Microbiology 2002
Pynciau:
Nucleocytoplasmic Communication
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC134221/
https://ncbi.nlm.nih.gov/pubmed/11739738
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.22.1.245-256.2002
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spelling pubmed-1342212003-01-08 Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes Wiegand, Heather L. Coburn, Glen A. Zeng, Yan Kang, Yibin Bogerd, Hal P. Cullen, Bryan R. Mol Cell Biol Nucleocytoplasmic Communication The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained unclear how Tap activity is regulated in vivo. Here, we report that the small NXT1/p15-1 protein functions as a critical cofactor for Tap-mediated mRNA export in both human and invertebrate cells. In the absence of NXT1 binding, the Tap protein is unable to effectively interact with components of the nuclear pore complex and both Tap nucleocytoplasmic shuttling and the nuclear export of mRNA molecules tethered to Tap are therefore severely attenuated. Formation of a Tap/NXT1 heterodimer enhances nucleoporin binding both in vitro and in vivo and induces the formation of a Tap/NXT1/nucleoporin ternary complex that is likely to be a key intermediate in the process of nuclear mRNA export. The critical importance of NXT1 for the nuclear export of poly(A)(+) RNA is emphasized by the finding that specific inhibition of the expression of the Drosophila homolog of human NXT1, by using RNA interference, results in the nuclear accumulation of poly(A)(+) RNA in cultured insect cells. These data suggest that NXT1 may act as a molecular switch that regulates the ability of Tap to mediate nuclear mRNA export by controlling the interaction of Tap with components of the nuclear pore. American Society for Microbiology 2002-01 /pmc/articles/PMC134221/ /pubmed/11739738 http://dx.doi.org/10.1128/MCB.22.1.245-256.2002 Text en Copyright © 2002, American Society for Microbiology
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Nucleocytoplasmic Communication
spellingShingle Nucleocytoplasmic Communication
Wiegand, Heather L.
Coburn, Glen A.
Zeng, Yan
Kang, Yibin
Bogerd, Hal P.
Cullen, Bryan R.
Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
description The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained unclear how Tap activity is regulated in vivo. Here, we report that the small NXT1/p15-1 protein functions as a critical cofactor for Tap-mediated mRNA export in both human and invertebrate cells. In the absence of NXT1 binding, the Tap protein is unable to effectively interact with components of the nuclear pore complex and both Tap nucleocytoplasmic shuttling and the nuclear export of mRNA molecules tethered to Tap are therefore severely attenuated. Formation of a Tap/NXT1 heterodimer enhances nucleoporin binding both in vitro and in vivo and induces the formation of a Tap/NXT1/nucleoporin ternary complex that is likely to be a key intermediate in the process of nuclear mRNA export. The critical importance of NXT1 for the nuclear export of poly(A)(+) RNA is emphasized by the finding that specific inhibition of the expression of the Drosophila homolog of human NXT1, by using RNA interference, results in the nuclear accumulation of poly(A)(+) RNA in cultured insect cells. These data suggest that NXT1 may act as a molecular switch that regulates the ability of Tap to mediate nuclear mRNA export by controlling the interaction of Tap with components of the nuclear pore.
author Wiegand, Heather L.
Coburn, Glen A.
Zeng, Yan
Kang, Yibin
Bogerd, Hal P.
Cullen, Bryan R.
author_facet Wiegand, Heather L.
Coburn, Glen A.
Zeng, Yan
Kang, Yibin
Bogerd, Hal P.
Cullen, Bryan R.
author_sort Wiegand, Heather L.
title Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
title_short Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
title_full Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
title_fullStr Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
title_full_unstemmed Formation of Tap/NXT1 Heterodimers Activates Tap-Dependent Nuclear mRNA Export by Enhancing Recruitment to Nuclear Pore Complexes
title_sort formation of tap/nxt1 heterodimers activates tap-dependent nuclear mrna export by enhancing recruitment to nuclear pore complexes
publisher American Society for Microbiology
publisher_facet American Society for Microbiology
publishDate 2002
url https://ncbi.nlm.nih.gov/pmc/articles/PMC134221/
https://ncbi.nlm.nih.gov/pubmed/11739738
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.22.1.245-256.2002
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