Structural basis for assembly and disassembly of the CRM1 nuclear export complex

CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1).

[1]  C. Dargemont,et al.  Evidence for a role of CRM1 in signal-mediated nuclear protein export. , 1997, Science.

[2]  Jørgen Kjems,et al.  The Specificity of the CRM1-Rev Nuclear Export Signal Interaction Is Mediated by RanGTP* , 1998, The Journal of Biological Chemistry.

[3]  Montserrat Soler-López,et al.  Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. , 2004, Molecular cell.

[4]  Yoshiyuki Matsuura,et al.  Structural basis for the assembly of a nuclear export complex , 2004, Nature.

[5]  Karsten Weis,et al.  Exportin 1 (Crm1p) Is an Essential Nuclear Export Factor , 1997, Cell.

[6]  F. Bischoff,et al.  CRM1-mediated Recycling of Snurportin 1 to the Cytoplasm , 1999, The Journal of cell biology.

[7]  Minoru Yoshida,et al.  CRM1 is responsible for intracellular transport mediated by the nuclear export signal , 1997, Nature.

[8]  U. Kutay,et al.  Transport between the cell nucleus and the cytoplasm. , 1999, Annual review of cell and developmental biology.

[9]  Minoru Yoshida,et al.  CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals , 1997, Cell.

[10]  M. Fornerod,et al.  Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358 , 2004, The EMBO journal.

[11]  Graydon B. Gonsalvez,et al.  Cross-talk between snurportin1 subdomains. , 2005, Molecular biology of the cell.

[12]  Achim Dickmanns,et al.  Structural basis for m3G‐cap‐mediated nuclear import of spliceosomal UsnRNPs by snurportin1 , 2005, The EMBO journal.

[13]  Yuh Min Chook,et al.  Structural basis for leucine-rich nuclear export signal recognition by CRM1 , 2009, Nature.

[14]  G. Cingolani,et al.  Molecular Basis for the Recognition of Snurportin 1 by Importin β* , 2008, Journal of Biological Chemistry.

[15]  Mitsuo Sekine,et al.  Snurportin1, an m3G‐cap‐specific nuclear import receptor with a novel domain structure , 1998, The EMBO journal.