Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import.

Abstract:

:In yeast there are at least 14 members of the beta-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 beta-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.

journal_name

Mol Cell Biol

authors

Leslie DM,Zhang W,Timney BL,Chait BT,Rout MP,Wozniak RW,Aitchison JD

doi

10.1128/MCB.24.19.8487-8503.2004

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

8487-503

issue

19

eissn

0270-7306

issn

1098-5549

pii

24/19/8487

journal_volume

24

pub_type

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