J. Biochem, 2004, Vol. 135, No. 2 201-216
© 2004 The Japanese Biochemical Society
CELL |
Dynamics of Golgi Matrix Proteins after the Blockage of ER to Golgi Transport
,1,21 Molecular Biology Laboratory, Faculty of Pharmaceutical Sciences, and 2 Cancer Research Institute, Kanazawa University, Kanazawa 920-0934; 3 Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582; 4 Department of Physiology, Kansai medical University, Moriguchi, Osaka 570-8506; 5 Department of Cell Biology, Fukuoka University School of Medicine, Fukuoka 814-0180; 6 Department of Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18a, Martinsried, D-82152, Germany; and 7 RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa 230-0045
When the ER to Golgi transport is blocked by a GTP-restricted mutant of Sar1p (H79G) in NRK-52E cells, most Golgi resident proteins are transported back into the ER. In contrast, the cis-Golgi matrix proteins GM130 and GRASP65 are retained in punctate cytoplasmic structures, namely Golgi remnants. Significant amounts of the medial-Golgi matrix proteins golgin-45, GRASP55 and giantin are retained in the Golgi remnants, but a fraction of these proteins relocates to the ER. Golgin-97, a candidate trans-Golgi network matrix protein, is retained in Golgi remnant-like structures, but mostly separated from GM130 and GRASP65. Interestingly, most Sec13p, a COPII component, congregates into larger cytoplasmic clusters soon after the microinjection of Sar1p(H79G), and these move to accumulate around the Golgi apparatus. Sec13p clusters remain associated with Golgi remnants after prolonged incubation. Electron microscopic analysis revealed that Golgi remnants are clusters of larger vesicles with smaller vesicles, many of which are coated. GM130 is mainly associated with larger vesicles and Sec13p with smaller coated vesicles. The Sec13p clusters disperse when p115 binding to the Golgi apparatus is inhibited. These results suggest that cis-Golgi matrix proteins resist retrograde transport flow and stay as true residents in Golgi remnants after the inhibition of ER to Golgi transport.
* Present address: Cell Biology Laboratory, Nagahama Institute of Bio-Science and Technology, 1266 Tamuramachi, Nagahama, Shiga 526-0829.
To whom correspondence should be addressed at: Molecular Biology Laboratory, Faculty of Pharmaceutical Sciences, Kanazawa University. Tel: +81-76-234-4466, Fax: +81-76-234-4467, E-mail: osaru3{at}kenroku.kanazawa-u.ac.jp
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