Vesicles on strings: Morphological evidence for processive transport within the Golgi stack Journal Article


Authors: Orci, L.; Perrelet, A.; Rothman, J. E.
Article Title: Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
Abstract: Cis-Golgi cisternae have a higher freeze-fracture particle density than trans-cisternae. Transport vesicles neighboring cis or trans positions of the Golgi stack have a particle concentration comparable to that of the adjacent cisterna and the buds emerging from it. This implies that transport vesicles remain locally within the stack during their lifetime, near their origin, favoring a processive pattern of transport in which vesicle transfers occur preferentially between adjacent cisternae in the stack. A 'string theory' is proposed to account for processive transport, in which a carpet of fibrous attachment proteins located at the surface of cisternae (the strings) prevent budded vesicles from diffusing away but still allow them to diffuse laterally, effectively limiting transfers to adjoining cisternae in the stack. Fibrous elements that multivalently connect otherwise free COPI- coated vesicles and uncoated transport vesicles to one or two cisternae simultaneously are discerned readily by electron microscopy. It is suggested that long, coiled coil, motif-rich, Golgi-specific proteins including p115, GM130, and possibly giantin, among others, function as the proposed strings.
Keywords: nonhuman; conference paper; animal cell; electron microscopy; animals; microscopy, electron; cell structure; cell protein; membrane proteins; intracellular transport; protein processing; adenosine triphosphate; cytosol; golgi complex; cho cells; cricetinae; membrane vesicle; intracellular membranes; coatomer protein; coated vesicles; golgi apparatus; intracellular membrane; priority journal; freeze-fracture; freeze fracturing
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 95
Issue: 5
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1998-03-03
Start Page: 2279
End Page: 2283
Language: English
DOI: 10.1073/pnas.95.5.2279
PUBMED: 9482876
PROVIDER: scopus
PMCID: PMC19319
DOI/URL:
Notes: Conference Paper -- Export Date: 12 December 2016 -- Source: Scopus
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  1. James E Rothman
    120 Rothman