Interactions between a Nuclear Transporter and a Subset of Nuclear Pore Complex Proteins Depend on Ran GTPase

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Molecular and Cellular Biology, February 1999, p. 1547-1557, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Interactions between a Nuclear Transporter and a Subset of Nuclear Pore Complex Proteins Depend on Ran GTPase

Matthias Seedorf, Marc Damelin, Jason Kahana, Tetsuya Taura, and Pamela A. Silver^*

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and The Dana-Farber Cancer Institute, Boston, Massachusetts 02115

Received 12 August 1998/Returned for modification 12 October 1998/Accepted 28 October 1998

Proteins to be transported into the nucleus are recognized by members of the importin-karyopherin nuclear transport receptorfamily. After docking at the nuclear pore complex (NPC), the cargo-receptorcomplex moves through the aqueous pore channel. Once cargo isreleased, the importin then moves back through the channel fornew rounds of transport. Thus, importin and exportin, anothermember of this family involved in export, are thought to continuouslyshuttle between the nuclear interior and the cytoplasm. In orderto understand how nuclear transporters traverse the NPC, we constructedfunctional protein fusions between several members of the yeastimportin family, including Pse1p, Sxm1p, Xpo1p, and Kap95p, andthe green fluorescent protein (GFP). Complexes containing nucleartransporters were isolated by using highly specific anti-GFP antibodies.Pse1-GFP was studied in the most detail. Pse1-GFP is in a complexwith importin- $alpha$ and - $beta$ (Srp1p and Kap95p in yeast cells) thatis sensitive to the nucleotide-bound state of the Ran GTPase.In addition, Pse1p associates with the nucleoporins Nsp1p, Nup159p,and Nup116p, while Sxm1p, Xpo1p, and Kap95p show different patternsof interaction with nucleoporins. Association of Pse1p with nucleoporinsalso depends on the nucleotide-bound state of Ran; when Ran isin the GTP-bound state, the nucleoporin association is lost. Amutant form of Pse1p that does not bind Ran also fails to interactwith nucleoporins. These data indicate that transport receptorssuch as Pse1p interact in a Ran-dependent manner with certainnucleoporins. These nucleoporins may represent major docking sitesfor Pse1p as it moves in or out of the nucleus via theNPC.

^* Corresponding author. Mailing address: The Dana-Farber Cancer Institute, 44 Binney St., Boston, MA 02115. Phone: (617) 632-5102.Fax: (617) 632-5103. E-mail: pfas.harvard.silver{at}edu.

Present address: ZMBH, Im Neuenheimer Feld 282, D-69120 Heidelberg,Germany.

Present address: Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla,Calif.

Molecular and Cellular Biology, February 1999, p. 1547-1557, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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