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

doi:10.1126/science.279.5350.573

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

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263 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	573-577
Number of pages	5
Journal	Science
Volume	279
Issue number	5350
DOIs	https://doi.org/10.1126/science.279.5350.573
State	Published - Jan 23 1998

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title = "Role of dynamin in the formation of transport vesicles from the trans- Golgi network",

abstract = "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.",

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T1 - Role of dynamin in the formation of transport vesicles from the trans- Golgi network

AU - Jones, Steven M.

AU - Howell, Kathryn E.

AU - Henley, John R.

AU - Cao, Hong

AU - McNiven, Mark A.

PY - 1998/1/23

Y1 - 1998/1/23

N2 - 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.

AB - 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.

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Role of dynamin in the formation of transport vesicles from the trans- Golgi network

Abstract

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