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Science 23 January 1998: Vol. 279. no. 5350, pp. 573 - 577 DOI: 10.1126/science.279.5350.573
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Reports
Role of Dynamin in the Formation of Transport Vesicles from the Trans-Golgi Network
Steven M. Jones,
Kathryn E. Howell,
John
R. Henley,
Hong Cao,
Mark A. McNiven
*
Dynamin guanosine triphosphatases support the scission of
clathrin-coated vesicles from the plasmalemma during endocytosis. By
fluorescence microscopy of cultured rat hepatocytes, a green fluorescent protein-dynamin II fusion protein localized with
clathrin-coated vesicles at the Golgi complex. A cell-free assay was
utilized to demonstrate the role of dynamin in vesicle formation at the trans-Golgi. Addition of peptide-specific anti-dynamin antibodies to
the assay mixture inhibited both constitutive exocytic and clathrin-coated vesicle formation. Immunodepletion of dynamin proteins
also inhibited vesicle formation, and budding efficiency was restored
upon readdition of purified dynamin. These data suggest that dynamin
participates in the formation of distinct transport vesicles from the
trans-Golgi network.
J. R. Henley, H. Cao, M. A. McNiven, Center for Basic
Research in Digestive Diseases, Mayo Clinic and Foundation, Rochester,
MN 55905, USA.
S. M. Jones, K. E. Howell, Department of Cellular & Structural Biology, University of Colorado School of Medicine, 4200 East 9th Avenue, Denver, CO 80262, USA.
*
To whom correspondence should be addressed. E-mail:
mcniven.mark{at}mayo.edu
Read the Full Text
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