RanBP3 influences interactions between CRM1 and its nuclear protein export substrates

Ludwig Englmeier, Maarten Fornerod, F. Ralf Bischoff, Carlo Petosa, Iain W. Mattaj*, Ulrike Kutay

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

98 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)926-932
Number of pages7
JournalEMBO Reports
Issue number10
Publication statusPublished - 1 Oct 2001
Externally publishedYes


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