Leucine-rich nuclear-export signals: born to be weak.
CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.
Kutay
Ulrike
U
Swiss Federal Institute of Technology (ETH) Zürich, Institute of Biochemistry, Schafmattstrasse 18, HPM F11.1, 8093 Zürich, Switzerland. ulrike.kutay@bc.biol.ethz.ch
Güttinger
Stephan
S
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D028884:Karyopherins / Q000502:physiology; D007930:Leucine / Q000737:chemistry*; D008954:Models, Biological; D008969:Molecular Sequence Data; D022022:Nuclear Pore / Q000378:metabolism; D018160:Receptors, Cytoplasmic and Nuclear / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D000097606:Exportin 1 Protein
D028884:Karyopherins; D007930:Leucine; D018160:Receptors, Cytoplasmic and Nuclear; D000097606:Exportin 1 Protein