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Published 20 December 2004. doi:10.1083/jcb.200409149
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 6, 1051-1062
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Article

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

Tomoyuki Ohba1,2, Eric C. Schirmer1, Takeharu Nishimoto2, and Larry Gerace1

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan

Correspondence to Larry Gerace: lgerace{at}scripps.edu

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.

E.C. Schirmer's present address is The Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, UK.

Abbreviations used in this paper: BAPTA-AM, 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetrakis (acetoxymethyl) ester; CHL, chicken hepatic lectin; FKBP, FK506-binding protein; FRB, FKBP-rapamycin binding domain; INM, inner nuclear membrane; LAP2ß, lamina-associated polypeptide 2ß; NE, nuclear envelope; NEM, N-ethylmaleimide; NPC, nuclear pore complex; ONM, outer nuclear membrane; PK, pyruvate kinase; VSV, vesicular stomatitis virus.


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