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Efficient Nuclear Transport of Structurally Disturbed Cargo: Mutations in a Cargo Protein Switch Its Cognate Karyopherin 1 2¤ Susana R. Chaves *, Jonathan S. Rosenblum 1 Centre of Molecular and Environmental Biology, Department of Biology, University of Minho, Campus de Gualtar, Braga, Portugal, 2 Howard Hughes Medical Institute, Laboratory of Cell Biology, The Rockefeller University, New York, New York, United States of America Abstract The Karyopherin (Kap) family of nuclear transport receptors enables trafficking of proteins to and from the nucleus in a precise, regulated manner. Individual members function in overlapping pathways, while simultaneously being very specific for their main cargoes. The details of this apparent contradiction and rules governing pathway preference remain to be further elucidated. S. cerevisiae Lhp1 is an abundant protein that functions as an RNA chaperone in a variety of biologically important processes. It localizes almost exclusively to the nucleus and is imported by Kap108. We show that mutation of 3 of the 275 residues in Lhp1 alters its import pathway to a Kap121-dependent process. This mutant does not retain wild-type function and is bound by several chaperones. We propose that Kap121 also acts as a chaperone, one that can act as a genetic buffer by transporting mutated proteins to the nucleus. Citation: Chaves SR, Rosenblum JS (2011) Efficient Nuclear Transport of Structurally Disturbed Cargo: Mutations in a Cargo Protein Switch Its Cognate Karyopherin. PLoS ONE 6(2): e16846. doi:10.1371/journal.pone.0016846 Editor: Janine Santos, University of Medicine and Dentistry of New Jersey, United States of America Received September 2, 2010; Accepted January 16, 2011; Published February 9, 2011 Copyright: 2011 Chaves, Rosenblum. This is an open-access