Possible Involvement of Heterotrimeric G Proteins in the Organization of the Golgi Apparatus*
- Tomohiro Yamaguchi‡§,
- Akitsugu Yamamoto¶,
- Akiko Furuno§,
- Kiyotaka Hatsuzawa§,
- Katsuko Tani§,
- Masaru Himeno‡ and
- Mitsuo Tagaya§‖
- From the ‡Division of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-82, Japan, the ¶Department of Physiology, Kansai Medical University, Moriguchi, Osaka 570, Japan, and the§School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Tokyo 192-03, Japan
Abstract
Nordihydroguaiaretic acid (NDGA) caused disassembly of the Golgi apparatus of NRK cells in a dose-, time-, and energy-dependent manner but not in a microtubule-dependent manner. In contrast to brefeldin A, NDGA did not cause release of β-COP, a component of Golgi-derived vesicles. However, NDGA-induced disassembly was blocked by AlF4 −, an activator of the heterotrimeric but not the small GTP-binding proteins. In digitonin-permeabilized cells, guanosine 5′-3-O-(thio)triphosphate (GTPγS) as well as AlF4 − blocked the NDGA-promoted disassembly of the Golgi apparatus, and Gβγ (βγ subunits of heterotrimeric G proteins) reversed this effect. Our present results suggest the possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus.
Footnotes
-
↵* This work was supported in part by grants-in-aid for scientific research from the Ministry of Education, Science, Sports and Culture of Japan and by the Yamada Science Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
-
↵‖ To whom all correspondence should be addressed. Tel.: 81-426-76-7110; Fax: 81-426-76-8866; E-mail:tagaya{at}ls.toyaku.ac.jp.
-
↵1 The abbreviations used are: NSF,N-ethylmaleimide-sensitive factor; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor; NDGA, nordihydroguaiaretic acid; ER, endoplasmic reticulum; Gαβγ, αβγ subunits of heterotrimeric G proteins; Man II, mannosidase II; IQ, ilimaquinone; GTPγS, guanosine 5′-3-O-(thio)triphosphate; ATPγS, adenosine 5′-O-(thiotriphosphate); AMPPNP, adenosine 5′-(β,γ-imino)triphosphate; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid; COP, coat protein; C6-NBD-ceramide, 6-((N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)aminocaproyl)sphingosine; WGA, wheat germ agglutinin.
-
↵2 Y. Ikehara, personal communication.
-
- Received February 6, 1997.
- Revision received July 1, 1997.
