{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T01:49:54Z","timestamp":1776822594158,"version":"3.51.2"},"reference-count":49,"publisher":"Proceedings of the National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2005,6,14]]},"abstract":"<jats:p>Human guanylate-binding protein-1 (hGBP-1) is a large GTPase, similar in structure to the dynamins. Like many smaller GTPases of the Ras\/Rab family, it is farnesylated, suggesting it may dock into membranes and perhaps play a role in intracellular trafficking. To date, however, hGBP-1 has never been associated with a specific intracellular compartment. Here we present evidence that hGBP-1 can associate with the Golgi apparatus. Redistribution from the cytosol to the Golgi was observed by immunofluorescence and subcellular fractionation after aluminum fluoride treatment, suggesting that it occurs when hGBP-1 is in its GTP-bound state. Relocalization was blocked by a farnesyl transferase inhibitor. The C589S mutant of hGBP-1, which cannot be farnesylated, and the previously uncharacterized R48P mutant, which cannot bind GTP, both failed to localize to the Golgi. These two mutants had a dominant-negative effect, preventing endogenous wild-type hGBP-1 from efficiently redistributing after aluminum fluoride treatment. Furthermore, hGBP-1 requires another IFN-\u03b3-induced factor to be targeted to the Golgi, because constitutively expressed hGBP-1 remained cytosolic in cells treated with aluminum fluoride unless the cells were preincubated with IFN-\u03b3. Finally, two nonhydrolyzing mutants of hGBP-1, corresponding to active mutants of Ras family proteins, failed to constitutively associate with the Golgi; we propose three possible explanations for this surprising result.<\/jats:p>","DOI":"10.1073\/pnas.0503227102","type":"journal-article","created":{"date-parts":[[2005,6,4]],"date-time":"2005-06-04T00:24:58Z","timestamp":1117844698000},"page":"8680-8685","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":72,"title":["Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-\u03b3-inducible cofactor"],"prefix":"10.1073","volume":"102","author":[{"given":"Nir","family":"Modiano","sequence":"first","affiliation":[{"name":"Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06520-8011"}]},{"given":"Yanping E.","family":"Lu","sequence":"additional","affiliation":[{"name":"Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06520-8011"}]},{"given":"Peter","family":"Cresswell","sequence":"additional","affiliation":[{"name":"Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06520-8011"}]}],"member":"341","published-online":{"date-parts":[[2005,6,3]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/19.17.4555"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/35000617"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.37.22310"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/20.20.5568"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg382"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9440(10)64452-5"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1999.9614"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(84)90016-3"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(85)90160-6"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0955-0674(99)80067-2"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(06)00295-8"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.8.4392"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.273.5271.115"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.134.4.935"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)36836-9"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/nm0895-792"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(94)90308-5"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0955-0674(99)00072-1"},{"key":"e_1_3_2_19_2","first-page":"611","volume":"6","year":"1994","unstructured":"Kaplan, J. 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