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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.
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