RanBP3 influences interactions between CRM1 and its nuclear protein export substrates |
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| Authors: | Englmeier L Fornerod M Bischoff F R Petosa C Mattaj I W Kutay U |
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| Affiliation: | European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. |
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| Abstract: | 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. |
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