Molecular and Cellular Biology, October 2004, p. 8487-8503, Vol. 24, No. 19
0270-7306/04/$08.00+0 DOI: 10.1128/MCB.24.19.8487-8503.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Characterization of Karyopherin Cargoes Reveals Unique Mechanisms of Kap121p-Mediated Nuclear Import
Deena M. Leslie,1,2 Wenzhu Zhang,3 Benjamin L. Timney,3 Brian T. Chait,3 Michael P. Rout,3 Richard W. Wozniak,2* and John D. Aitchison2*
Institute for Systems Biology, Seattle, Washington,1
Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada,2
The Rockefeller University, New York, New York3
Received 2 February 2004/
Returned for modification 8 March 2004/
Accepted 30 June 2004
In yeast there are at least 14 members of the ß-karyopherin protein family that govern the movement of a diverse set of cargoes between the nucleus and cytoplasm. Knowledge of the cargoes carried by each karyopherin and insight into the mechanisms of transport are fundamental to understanding constitutive and regulated transport and elucidating how they impact normal cellular functions. Here, we have focused on the identification of nuclear import cargoes for the essential yeast ß-karyopherin, Kap121p. Using an overlay blot assay and coimmunopurification studies, we have identified 30 putative Kap121p cargoes. Among these were Nop1p and Sof1p, two essential trans-acting protein factors required at the early stages of ribosome biogenesis. Characterization of the Kap121p-Nop1p and Kap121p-Sof1p interactions demonstrated that, in addition to lysine-rich nuclear localization signals (NLSs), Kap121p recognizes a unique class of signals distinguished by the abundance of arginine and glycine residues and consequently termed rg-NLSs. Kap104p is also known to recognize rg-NLSs, and here we show that it compensates for the loss of Kap121p function. Sof1p is also transported by Kap121p; however, its import can be mediated by a piggyback mechanism with Nop1p bridging the interaction between Sof1p and Kap121p. Together, our data elucidate additional levels of complexity in these nuclear transport pathways.
* Corresponding author. Mailing address for Richard W. Wozniak: Department of Cell Biology, MSB 5-14, University of Alberta, Edmonton, AB T6G 2H7, Canada. Phone: (708) 492-1384. Fax: (780) 492-0450. E-mail: rick.wozniak{at}ualberta.ca. Mailing address for John D. Aitchison: Institute for Systems Biology, 1441 N 34th St., Seattle, WA 98103. Phone: (206) 732-1344. Fax: (206) 732-1299. E-mail: jaitchison{at}systemsbiology.org.
Molecular and Cellular Biology, October 2004, p. 8487-8503, Vol. 24, No. 19
0022-538X/04/$08.00+0 DOI: 10.1128/MCB.24.19.8487-8503.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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Copyright © 2004 by the American Society for Microbiology. All rights reserved.