Structural basis for cargo regulation of COPII coat assembly. Export

@article{citeulike:3276052, abstract = {Using cryo-electron microscopy, we have solved the structure of an icosidodecahedral COPII coat involved in cargo export from the endoplasmic reticulum (ER) coassembled from purified cargo adaptor Sec23-24 and Sec13-31 lattice-forming complexes. The coat structure shows a tetrameric assembly of the Sec23-24 adaptor layer that is well positioned beneath the vertices and edges of the Sec13-31 lattice. Fitting the known crystal structures of the COPII proteins into the density map reveals a flexible hinge region stemming from interactions between WD40 beta-propeller domains present in Sec13 and Sec31 at the vertices. The structure shows that the hinge region can direct geometric cage expansion to accommodate a wide range of bulky cargo, including procollagen and chylomicrons, that is sensitive to adaptor function in inherited disease. The COPII coat structure leads us to propose a mechanism by which cargo drives cage assembly and membrane curvature for budding from the ER.}, address = {National Resource for Automated Molecular Microscopy, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.}, author = {Stagg, S. M. and LaPointe, P. and Razvi, A. and G\"{u}rkan, C. and Potter, C. S. and Carragher, B. and Balch, W. E.}, citeulike-article-id = {3276052}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2008.06.024}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18692470}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18692470}, day = {8}, doi = {10.1016/j.cell.2008.06.024}, issn = {1097-4172}, journal = {Cell}, keywords = {budding, complexes, copii}, month = {August}, number = {3}, pages = {474--484}, posted-at = {2008-09-16 21:47:31}, priority = {2}, title = {Structural basis for cargo regulation of COPII coat assembly.}, url = {http://dx.doi.org/10.1016/j.cell.2008.06.024}, volume = {134}, year = {2008} }

TY - JOUR ID - citeulike:3276052 L3 - citeulike-article-id:3276052 N2 - Using cryo-electron microscopy, we have solved the structure of an icosidodecahedral COPII coat involved in cargo export from the endoplasmic reticulum (ER) coassembled from purified cargo adaptor Sec23-24 and Sec13-31 lattice-forming complexes. The coat structure shows a tetrameric assembly of the Sec23-24 adaptor layer that is well positioned beneath the vertices and edges of the Sec13-31 lattice. Fitting the known crystal structures of the COPII proteins into the density map reveals a flexible hinge region stemming from interactions between WD40 beta-propeller domains present in Sec13 and Sec31 at the vertices. The structure shows that the hinge region can direct geometric cage expansion to accommodate a wide range of bulky cargo, including procollagen and chylomicrons, that is sensitive to adaptor function in inherited disease. The COPII coat structure leads us to propose a mechanism by which cargo drives cage assembly and membrane curvature for budding from the ER. IS - 3 JF - Cell SN - 1097-4172 AD - National Resource for Automated Molecular Microscopy, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. EP - 484 TI - Structural basis for cargo regulation of COPII coat assembly. VL - 134 SP - 474 KW - budding KW - complexes KW - copii AU - Stagg, SM AU - LaPointe, P AU - Razvi, A AU - Gürkan, C AU - Potter, CS AU - Carragher, B AU - Balch, WE PY - 2008/08/08/ UR - http://dx.doi.org/10.1016/j.cell.2008.06.024 ER -