© The Rockefeller University Press,
0021-9525/1997//1645 $5.00
The Journal of Cell Biology, Volume 139, Number 7,
, 1997 1645-1653
A Distinct and Parallel Pathway for the Nuclear Import of an mRNA-binding Protein
Lucy F. Pemberton,
Jonathan S. Rosenblum, and
Günter Blobel
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York 10021
Three independent pathways of nuclear import have so far been identified in yeast, each mediated by cognate nuclear transport factors, or karyopherins. Here we have characterized a new pathway to the nucleus, mediated by Mtr10p, a protein first identified in a screen for strains defective in polyadenylated RNA export. Mtr10p is shown to be responsible for the nuclear import of the shuttling mRNA-binding protein Npl3p. A complex of Mtr10p and Npl3p was detected in cytosol, and deletion of Mtr10p was shown to lead to the mislocalization of nuclear Npl3p to the cytoplasm, correlating with a block in import. Mtr10p bound peptide repeat-containing nucleoporins and Ran, suggesting that this import pathway involves a docking step at the nuclear pore complex and is Ran dependent. This pathway of Npl3p import is distinct and does not appear to overlap with another known import pathway for an mRNA-binding protein. Thus, at least two parallel pathways function in the import of mRNA-binding proteins, suggesting the need for the coordination of these pathways.
Abbreviations used in this paper: ADH, alcohol dehydrogenase; GFP, green fluorescent protein; GST, glutathione-S-transferase; hn, heterogeneous nuclear; NPC, nuclear pore complex.
J.S. Rosenblum was supported by a postdoctoral fellowship from the National Institutes of Health.
Address all correspondence to Günter Blobel, Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021. Tel.: (212) 327-8181. Fax: (212) 327-7880. E-mail: blobel @rockvax.rockefeller.edu

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