Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes

Kohji Takei, Volker Haucke, Vladimir Slepnev, Khashayar Farsad, Marco Salazar, Hong Chen, Pietro De Camilli

Research output: Contribution to journalArticle

282 Citations (Scopus)

Abstract

Clathrin-coated buds and dynamin-coated tubules morphologically similar to corresponding structures observed in synaptic membranes can be generated on protein-free liposomes by incubation with cytosol, or with clathrin coat proteins and purified dynamin, respectively. Dynamin- and clathrin-coated intermediates may form independently of each other, despite the coupling between the two processes typically observed in synaptic membranes. Formation of both structures on liposomes can occur in the absence of nucleotides. These findings indicate that interfaces between lipids and cytosolic proteins are fully sufficient to deform lipids bilayers into buds and tubules. They suggest that a main function of membrane proteins is to act as positive and negative regulators of coat assembly, therefore controlling these processes in time and space.

Original languageEnglish
Pages (from-to)131-141
Number of pages11
JournalCell
Volume94
Issue number1
DOIs
Publication statusPublished - Jul 10 1998
Externally publishedYes

Fingerprint

Dynamins
Clathrin
Endocytosis
Liposomes
Synaptic Membranes
Membranes
Proteins
Lipid bilayers
Capsid Proteins
Lipid Bilayers
Cytosol
Membrane Proteins
Nucleotides
Lipids

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Takei, K., Haucke, V., Slepnev, V., Farsad, K., Salazar, M., Chen, H., & De Camilli, P. (1998). Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell, 94(1), 131-141. https://doi.org/10.1016/S0092-8674(00)81228-3

Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. / Takei, Kohji; Haucke, Volker; Slepnev, Vladimir; Farsad, Khashayar; Salazar, Marco; Chen, Hong; De Camilli, Pietro.

In: Cell, Vol. 94, No. 1, 10.07.1998, p. 131-141.

Research output: Contribution to journalArticle

Takei, K, Haucke, V, Slepnev, V, Farsad, K, Salazar, M, Chen, H & De Camilli, P 1998, 'Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes', Cell, vol. 94, no. 1, pp. 131-141. https://doi.org/10.1016/S0092-8674(00)81228-3
Takei, Kohji ; Haucke, Volker ; Slepnev, Vladimir ; Farsad, Khashayar ; Salazar, Marco ; Chen, Hong ; De Camilli, Pietro. / Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. In: Cell. 1998 ; Vol. 94, No. 1. pp. 131-141.
@article{3d0c4a0b1d184c8da82d1bcd34befe68,
title = "Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes",
abstract = "Clathrin-coated buds and dynamin-coated tubules morphologically similar to corresponding structures observed in synaptic membranes can be generated on protein-free liposomes by incubation with cytosol, or with clathrin coat proteins and purified dynamin, respectively. Dynamin- and clathrin-coated intermediates may form independently of each other, despite the coupling between the two processes typically observed in synaptic membranes. Formation of both structures on liposomes can occur in the absence of nucleotides. These findings indicate that interfaces between lipids and cytosolic proteins are fully sufficient to deform lipids bilayers into buds and tubules. They suggest that a main function of membrane proteins is to act as positive and negative regulators of coat assembly, therefore controlling these processes in time and space.",
author = "Kohji Takei and Volker Haucke and Vladimir Slepnev and Khashayar Farsad and Marco Salazar and Hong Chen and {De Camilli}, Pietro",
year = "1998",
month = "7",
day = "10",
doi = "10.1016/S0092-8674(00)81228-3",
language = "English",
volume = "94",
pages = "131--141",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "1",

}

TY - JOUR

T1 - Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes

AU - Takei, Kohji

AU - Haucke, Volker

AU - Slepnev, Vladimir

AU - Farsad, Khashayar

AU - Salazar, Marco

AU - Chen, Hong

AU - De Camilli, Pietro

PY - 1998/7/10

Y1 - 1998/7/10

N2 - Clathrin-coated buds and dynamin-coated tubules morphologically similar to corresponding structures observed in synaptic membranes can be generated on protein-free liposomes by incubation with cytosol, or with clathrin coat proteins and purified dynamin, respectively. Dynamin- and clathrin-coated intermediates may form independently of each other, despite the coupling between the two processes typically observed in synaptic membranes. Formation of both structures on liposomes can occur in the absence of nucleotides. These findings indicate that interfaces between lipids and cytosolic proteins are fully sufficient to deform lipids bilayers into buds and tubules. They suggest that a main function of membrane proteins is to act as positive and negative regulators of coat assembly, therefore controlling these processes in time and space.

AB - Clathrin-coated buds and dynamin-coated tubules morphologically similar to corresponding structures observed in synaptic membranes can be generated on protein-free liposomes by incubation with cytosol, or with clathrin coat proteins and purified dynamin, respectively. Dynamin- and clathrin-coated intermediates may form independently of each other, despite the coupling between the two processes typically observed in synaptic membranes. Formation of both structures on liposomes can occur in the absence of nucleotides. These findings indicate that interfaces between lipids and cytosolic proteins are fully sufficient to deform lipids bilayers into buds and tubules. They suggest that a main function of membrane proteins is to act as positive and negative regulators of coat assembly, therefore controlling these processes in time and space.

UR - http://www.scopus.com/inward/record.url?scp=0032503947&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032503947&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(00)81228-3

DO - 10.1016/S0092-8674(00)81228-3

M3 - Article

VL - 94

SP - 131

EP - 141

JO - Cell

JF - Cell

SN - 0092-8674

IS - 1

ER -