Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore

Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism. To study this transport, we developed a live cell a...

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Main Authors:	Ohba, Tomoyuki, Schirmer, Eric C., Nishimoto, Takeharu, Gerace, Larry
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2004
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172626/

id	pubmed-2172626
recordtype	oai_dc
spelling	pubmed-21726262008-03-05 Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore Ohba, Tomoyuki Schirmer, Eric C. Nishimoto, Takeharu Gerace, Larry Research Articles Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism. To study this transport, we developed a live cell assay that measures the movement of transmembrane reporters from the ER to the INM by rapamycin-mediated trapping at the nuclear lamina. Reporter constructs with small (<30 kD) cytosolic and lumenal domains rapidly accumulated at the INM. However, increasing the size of either domain by 47 kD strongly inhibited movement. Reduced temperature and ATP depletion also inhibited movement, which is characteristic of membrane fusion mechanisms, but pharmacological inhibition of vesicular trafficking had no effect. Because reporter accumulation at the INM was inhibited by antibodies to the nuclear pore membrane protein gp210, our results support a model wherein transport of integral proteins to the INM involves lateral diffusion in the lipid bilayer around the nuclear pore membrane, coupled with active restructuring of the nuclear pore complex. The Rockefeller University Press 2004-12-20 /pmc/articles/PMC2172626/ /pubmed/15611332 http://dx.doi.org/10.1083/jcb.200409149 Text en Copyright © 2004, 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	Ohba, Tomoyuki Schirmer, Eric C. Nishimoto, Takeharu Gerace, Larry
spellingShingle	Ohba, Tomoyuki Schirmer, Eric C. Nishimoto, Takeharu Gerace, Larry Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
author_facet	Ohba, Tomoyuki Schirmer, Eric C. Nishimoto, Takeharu Gerace, Larry
author_sort	Ohba, Tomoyuki
title	Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
title_short	Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
title_full	Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
title_fullStr	Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
title_full_unstemmed	Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
title_sort	energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
description	Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism. To study this transport, we developed a live cell assay that measures the movement of transmembrane reporters from the ER to the INM by rapamycin-mediated trapping at the nuclear lamina. Reporter constructs with small (<30 kD) cytosolic and lumenal domains rapidly accumulated at the INM. However, increasing the size of either domain by 47 kD strongly inhibited movement. Reduced temperature and ATP depletion also inhibited movement, which is characteristic of membrane fusion mechanisms, but pharmacological inhibition of vesicular trafficking had no effect. Because reporter accumulation at the INM was inhibited by antibodies to the nuclear pore membrane protein gp210, our results support a model wherein transport of integral proteins to the INM involves lateral diffusion in the lipid bilayer around the nuclear pore membrane, coupled with active restructuring of the nuclear pore complex.
publisher	The Rockefeller University Press
publishDate	2004
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172626/
_version_	1611424994377596928

Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore

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