Structure of the Sec23p/24p and Sec13p/31p complexes of COPII. Export

@article{citeulike:5218259, abstract = {COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. We have used a combination of biochemistry and electron microscopy to investigate the molecular organization and structure of Sec23p/24p and Sec13p/31p complexes. The three-dimensional reconstruction of Sec23p/24p reveals that it has a bone-shaped structure, (17 nm in length), composed of two similar globular domains, one corresponding to Sec23p and the other to Sec24p. Sec13p/31p is a heterotetramer composed of two copies of Sec13p and two copies of Sec31p. It has an elongated shape, is 28-30 nm in length, and contains five consecutive globular domains linked by relatively flexible joints. Putting together the architecture of these Sec complexes with the interactions between their subunits and the appearance of the coat in COPII-coated vesicles, we present a model for COPII coat organization.}, author = {Lederkremer, G. Z. and Cheng, Y. and Petre, B. M. and Vogan, E. and Springer, S. and Schekman, R. and Walz, T. and Kirchhausen, T.}, citeulike-article-id = {5218259}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.191359398}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11535824}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11535824}, day = {11}, doi = {10.1073/pnas.191359398}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {copii, negative, structure, topology}, month = {September}, number = {19}, pages = {10704--10709}, posted-at = {2009-07-21 12:34:59}, priority = {2}, title = {Structure of the Sec23p/24p and Sec13p/31p complexes of COPII.}, url = {http://dx.doi.org/10.1073/pnas.191359398}, volume = {98}, year = {2001} }

TY - JOUR ID - citeulike:5218259 L3 - citeulike-article-id:5218259 N2 - COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. We have used a combination of biochemistry and electron microscopy to investigate the molecular organization and structure of Sec23p/24p and Sec13p/31p complexes. The three-dimensional reconstruction of Sec23p/24p reveals that it has a bone-shaped structure, (17 nm in length), composed of two similar globular domains, one corresponding to Sec23p and the other to Sec24p. Sec13p/31p is a heterotetramer composed of two copies of Sec13p and two copies of Sec31p. It has an elongated shape, is 28-30 nm in length, and contains five consecutive globular domains linked by relatively flexible joints. Putting together the architecture of these Sec complexes with the interactions between their subunits and the appearance of the coat in COPII-coated vesicles, we present a model for COPII coat organization. IS - 19 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 0027-8424 EP - 10709 TI - Structure of the Sec23p/24p and Sec13p/31p complexes of COPII. VL - 98 SP - 10704 KW - copii KW - negative KW - structure KW - topology AU - Lederkremer, GZ AU - Cheng, Y AU - Petre, BM AU - Vogan, E AU - Springer, S AU - Schekman, R AU - Walz, T AU - Kirchhausen, T PY - 2001/09/11/ UR - http://dx.doi.org/10.1073/pnas.191359398 ER -