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Lumenal interactions in nuclear pore complex assembly and stability

Nuclear pore complexes (NPCs) provide a gateway for the selective transport of macromolecules across the nuclear envelope (NE). Although we have a solid understanding of NPC composition and structure, we do not have a clear grasp of the mechanism of NPC assembly. Here, we demonstrate specific defect...

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Detalles Bibliográficos
Autores principales: Yewdell, William T., Colombi, Paolo, Makhnevych, Taras, Lusk, C. Patrick
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078075/
https://www.ncbi.nlm.nih.gov/pubmed/21346187
http://dx.doi.org/10.1091/mbc.E10-06-0554
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author Yewdell, William T.
Colombi, Paolo
Makhnevych, Taras
Lusk, C. Patrick
author_facet Yewdell, William T.
Colombi, Paolo
Makhnevych, Taras
Lusk, C. Patrick
author_sort Yewdell, William T.
collection PubMed
description Nuclear pore complexes (NPCs) provide a gateway for the selective transport of macromolecules across the nuclear envelope (NE). Although we have a solid understanding of NPC composition and structure, we do not have a clear grasp of the mechanism of NPC assembly. Here, we demonstrate specific defects in nucleoporin distribution in strains lacking Heh1p and Heh2p—two conserved members of the LEM (Lap2, emerin, MAN1) family of integral inner nuclear membrane proteins. These effects on nucleoporin localization are likely of functional importance as we have defined specific genetic interaction networks between HEH1 and HEH2, and genes encoding nucleoporins in the membrane, inner, and outer ring complexes of the NPC. Interestingly, expression of a domain of Heh1p that resides in the NE lumen is sufficient to suppress both the nucleoporin mislocalization and growth defects in heh1Δpom34Δ strains. We further demonstrate a specific physical interaction between the Heh1p lumenal domain and the massive cadherin-like lumenal domain of the membrane nucleoporin Pom152p. These findings support a role for Heh1p in the assembly or stability of the NPC, potentially through the formation of a lumenal bridge with Pom152p.
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spelling pubmed-30780752011-06-30 Lumenal interactions in nuclear pore complex assembly and stability Yewdell, William T. Colombi, Paolo Makhnevych, Taras Lusk, C. Patrick Mol Biol Cell Articles Nuclear pore complexes (NPCs) provide a gateway for the selective transport of macromolecules across the nuclear envelope (NE). Although we have a solid understanding of NPC composition and structure, we do not have a clear grasp of the mechanism of NPC assembly. Here, we demonstrate specific defects in nucleoporin distribution in strains lacking Heh1p and Heh2p—two conserved members of the LEM (Lap2, emerin, MAN1) family of integral inner nuclear membrane proteins. These effects on nucleoporin localization are likely of functional importance as we have defined specific genetic interaction networks between HEH1 and HEH2, and genes encoding nucleoporins in the membrane, inner, and outer ring complexes of the NPC. Interestingly, expression of a domain of Heh1p that resides in the NE lumen is sufficient to suppress both the nucleoporin mislocalization and growth defects in heh1Δpom34Δ strains. We further demonstrate a specific physical interaction between the Heh1p lumenal domain and the massive cadherin-like lumenal domain of the membrane nucleoporin Pom152p. These findings support a role for Heh1p in the assembly or stability of the NPC, potentially through the formation of a lumenal bridge with Pom152p. The American Society for Cell Biology 2011-04-15 /pmc/articles/PMC3078075/ /pubmed/21346187 http://dx.doi.org/10.1091/mbc.E10-06-0554 Text en © 2011 Yewdell et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,“ “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Yewdell, William T.
Colombi, Paolo
Makhnevych, Taras
Lusk, C. Patrick
Lumenal interactions in nuclear pore complex assembly and stability
title Lumenal interactions in nuclear pore complex assembly and stability
title_full Lumenal interactions in nuclear pore complex assembly and stability
title_fullStr Lumenal interactions in nuclear pore complex assembly and stability
title_full_unstemmed Lumenal interactions in nuclear pore complex assembly and stability
title_short Lumenal interactions in nuclear pore complex assembly and stability
title_sort lumenal interactions in nuclear pore complex assembly and stability
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078075/
https://www.ncbi.nlm.nih.gov/pubmed/21346187
http://dx.doi.org/10.1091/mbc.E10-06-0554
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AT luskcpatrick lumenalinteractionsinnuclearporecomplexassemblyandstability