Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport. Export

@article{citeulike:4491904, abstract = {GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.}, author = {Shiba, Tomoo and Kawasaki, Masato and Takatsu, Hiroyuki and Nogi, Terukazu and Matsugaki, Naohiro and Igarashi, Noriyuki and Suzuki, Mamoru and Kato, Ryuichi and Nakayama, Kazuhisa and Wakatsuki, Soichi}, citeulike-article-id = {4491904}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nsb920}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12679809}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12679809}, doi = {10.1038/nsb920}, issn = {1072-8368}, journal = {Nature structural biology}, keywords = {arf}, month = {May}, number = {5}, pages = {386--393}, posted-at = {2009-05-08 11:08:42}, priority = {2}, title = {Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.}, url = {http://dx.doi.org/10.1038/nsb920}, volume = {10}, year = {2003} }

TY - JOUR ID - citeulike:4491904 L3 - citeulike-article-id:4491904 N2 - GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP. IS - 5 JF - Nature structural biology SN - 1072-8368 EP - 393 TI - Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport. VL - 10 SP - 386 KW - arf AU - Shiba, Tomoo AU - Kawasaki, Masato AU - Takatsu, Hiroyuki AU - Nogi, Terukazu AU - Matsugaki, Naohiro AU - Igarashi, Noriyuki AU - Suzuki, Mamoru AU - Kato, Ryuichi AU - Nakayama, Kazuhisa AU - Wakatsuki, Soichi PY - 2003/05// UR - http://dx.doi.org/10.1038/nsb920 ER -