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Published 24 December 2001. doi:10.1083/jcb.200108073
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© The Rockefeller University Press, 0021-9525/2001/12/1225 $5.00
The Journal of Cell Biology, Volume 155, Number 7, December 24, 2001 1225-1238

Article

 Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae

Alexander A. Mironov1, Galina V. Beznoussenko1, Paolo Nicoziani1, Oliviano Martella1, Alvar Trucco1, Hee-Seok Kweon1, Daniele Di Giandomenico1, Roman S. Polishchuk1, Aurora Fusella1, Pietro Lupetti2, Eric G. Berger3, Willie J.C. Geerts4, Abraham J. Koster4, Koert N.J. Burger4 and Alberto Luini1

1 Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche "Mario Negri," 66030 Santa Maria Imbaro, Chieti, Italy
2 Dipartimento di Biologia Evolutiva, Università di Siena, 453100 Siena, Italy
3 Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland
4 Department of Molecular Cell Biology, Institute of Biomembranes, Utrecht University, 83584 CH Utrecht, Netherlands

Address correspondence to A. Luini, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Via Nazionale, 66030 Santa Maria Imbaro, Chieti, Italy. Tel.: 39-0872-570-323. Fax: 39-0872-570-412. E-mail: luini{at}dcbo.cmns.mnegri.it

Procollagen (PC)-I aggregates transit through the Golgi complex without leaving the lumen of Golgi cisternae. Based on this evidence, we have proposed that PC-I is transported across the Golgi stacks by the cisternal maturation process. However, most secretory cargoes are small, freely diffusing proteins, thus raising the issue whether they move by a transport mechanism different than that used by PC-I. To address this question we have developed procedures to compare the transport of a small protein, the G protein of the vesicular stomatitis virus (VSVG), with that of the much larger PC-I aggregates in the same cell. Transport was followed using a combination of video and EM, providing high resolution in time and space. Our results reveal that PC-I aggregates and VSVG move synchronously through the Golgi at indistinguishable rapid rates. Additionally, not only PC-I aggregates (as confirmed by ultrarapid cryofixation), but also VSVG, can traverse the stack without leaving the cisternal lumen and without entering Golgi vesicles in functionally relevant amounts. Our findings indicate that a common mechanism independent of anterograde dissociative carriers is responsible for the traffic of small and large secretory cargo across the Golgi stack.

Key Words: intracellular traffic; Golgi complex; transport vesicles; procollagen; VSVG


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