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RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
Author(s) -
Englmeier Ludwig,
Fornerod Maarten,
Bischoff F Ralf,
Petosa Carlo,
Mattaj Iain W,
Kutay Ulrike
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve200
Subject(s) - nuclear export signal , ran , nuclear protein , biology , microbiology and biotechnology , nuclear transport , cell nucleus , biochemistry , biophysics , nucleus , gene , transcription factor
We investigated the role of RanBP3, a nuclear member of the Ran‐binding protein 1 family, in CRM1‐mediated protein export in higher eukaryotes. RanBP3 interacts directly with CRM1 and also forms a trimeric complex with CRM1 and RanGTP. However, RanBP3 does not bind to CRM1 like an export substrate. Instead, it can stabilize CRM1–export substrate interaction. Nuclear RanBP3 stimulates CRM1‐dependent protein export in permeabilized cells. These data indicate that RanBP3 functions by a novel mechanism as a cofactor in recognition and export of certain CRM1 substrates. In vitro , RanBP3 binding to CRM1 affects the relative affinity of CRM1 for different substrates.