Golgicide A reveals essential roles for GBF1 in Golgi assembly and function. Export

@article{citeulike:4240091, abstract = {ADP ribosylation factor 1 (Arf1) plays a critical role in regulating secretory traffic and membrane transport within the Golgi of eukaryotic cells. Arf1 is activated by guanine nucleotide exchange factors (ArfGEFs), which confer spatial and temporal specificity to vesicular transport. We describe here the discovery and characterization of golgicide A, a potent, highly specific, reversible inhibitor of the cis-Golgi ArfGEF GBF1. Inhibition of GBF1 function resulted in rapid dissociation of COPI vesicle coat from Golgi membranes and subsequent disassembly of the Golgi and trans-Golgi network. Secretion of soluble and membrane-associated proteins was arrested at the endoplasmic reticulum-Golgi intermediate compartment, whereas endocytosis and recycling of transferrin were unaffected by GBF1 inhibition. Internalized shiga toxin was arrested within the endocytic compartment and was unable to reach the dispersed trans-Golgi network. Collectively, these results highlight the central role for GBF1 in coordinating bidirectional transport and maintaining structural integrity of the Golgi.}, author = {S\'{a}enz, J. B. and Sun, W. J. and Chang, J. W. and Li, J. and Bursulaya, B. and Gray, N. S. and Haslam, D. B.}, citeulike-article-id = {4240091}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nchembio.144}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19182783}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19182783}, doi = {10.1038/nchembio.144}, issn = {1552-4469}, journal = {Nature chemical biology}, keywords = {arf1, gbf1, gef, golgi, in\_vivo, interactions, membrane, regulation}, month = {March}, number = {3}, pages = {157--165}, posted-at = {2009-03-31 13:26:45}, priority = {2}, title = {Golgicide A reveals essential roles for GBF1 in Golgi assembly and function.}, url = {http://dx.doi.org/10.1038/nchembio.144}, volume = {5}, year = {2009} }

TY - JOUR ID - citeulike:4240091 L3 - citeulike-article-id:4240091 N2 - ADP ribosylation factor 1 (Arf1) plays a critical role in regulating secretory traffic and membrane transport within the Golgi of eukaryotic cells. Arf1 is activated by guanine nucleotide exchange factors (ArfGEFs), which confer spatial and temporal specificity to vesicular transport. We describe here the discovery and characterization of golgicide A, a potent, highly specific, reversible inhibitor of the cis-Golgi ArfGEF GBF1. Inhibition of GBF1 function resulted in rapid dissociation of COPI vesicle coat from Golgi membranes and subsequent disassembly of the Golgi and trans-Golgi network. Secretion of soluble and membrane-associated proteins was arrested at the endoplasmic reticulum-Golgi intermediate compartment, whereas endocytosis and recycling of transferrin were unaffected by GBF1 inhibition. Internalized shiga toxin was arrested within the endocytic compartment and was unable to reach the dispersed trans-Golgi network. Collectively, these results highlight the central role for GBF1 in coordinating bidirectional transport and maintaining structural integrity of the Golgi. IS - 3 JF - Nature chemical biology SN - 1552-4469 EP - 165 TI - Golgicide A reveals essential roles for GBF1 in Golgi assembly and function. VL - 5 SP - 157 KW - arf1 KW - gbf1 KW - gef KW - golgi KW - in_vivo KW - interactions KW - membrane KW - regulation AU - Sáenz, JB AU - Sun, WJ AU - Chang, JW AU - Li, J AU - Bursulaya, B AU - Gray, NS AU - Haslam, DB PY - 2009/03// UR - http://dx.doi.org/10.1038/nchembio.144 ER -