The binding of clathrin triskelions to membranes from coated vesicles

Emil R. Unanue; Ernst Ungewickell; Daniel Branton

doi:10.1016/0092-8674(81)90213-0

The binding of clathrin triskelions to membranes from coated vesicles

Emil R. Unanue, Ernst Ungewickell, Daniel Branton

Research output: Contribution to journal › Article › peer-review

102 Scopus citations

Abstract

We have developed a quantitative method to study the interaction of radiolabeled clathrin triskelions with membranes from brain coated vesicles. Clathrin triskelions do not bind to coated vesicles unless these are stripped of their clathrin coat. The binding of triskelions is of high affinity (K_D ≅ 2 × 10^-9 M), is saturable and depends on vesicle concentration. Triskelions bind to protein-sensitive structures of the stripped vesicles. Polypeptides of about 110,000 daltons appear to be involved in the binding structure. The association of triskelions to stripped vesicles was confirmed by electron microscopy.

Original language	English
Pages (from-to)	439-446
Number of pages	8
Journal	Cell
Volume	26
Issue number	3 PART 1
DOIs	https://doi.org/10.1016/0092-8674(81)90213-0
State	Published - Nov 1981

Access to Document

10.1016/0092-8674(81)90213-0

Cite this

@article{8d89df4b3ed243818531fcd9597715b0,

title = "The binding of clathrin triskelions to membranes from coated vesicles",

abstract = "We have developed a quantitative method to study the interaction of radiolabeled clathrin triskelions with membranes from brain coated vesicles. Clathrin triskelions do not bind to coated vesicles unless these are stripped of their clathrin coat. The binding of triskelions is of high affinity (KD ≅ 2 × 10-9 M), is saturable and depends on vesicle concentration. Triskelions bind to protein-sensitive structures of the stripped vesicles. Polypeptides of about 110,000 daltons appear to be involved in the binding structure. The association of triskelions to stripped vesicles was confirmed by electron microscopy.",

author = "Unanue, {Emil R.} and Ernst Ungewickell and Daniel Branton",

note = "Funding Information: Emil Unanue was supported in part by a grant from the Guggenheim Foundation while on sabbatical leave from Harvard University Medical School. Ernst Ungewickell was supported by a grant from the Deutsche Forschungsgemeinschaft. Research was supported in part by a grant from the National Institutes of Health.",

year = "1981",

month = nov,

doi = "10.1016/0092-8674(81)90213-0",

language = "English",

volume = "26",

pages = "439--446",

journal = "Cell",

issn = "0092-8674",

number = "3 PART 1",

}

TY - JOUR

T1 - The binding of clathrin triskelions to membranes from coated vesicles

AU - Unanue, Emil R.

AU - Ungewickell, Ernst

AU - Branton, Daniel

N1 - Funding Information: Emil Unanue was supported in part by a grant from the Guggenheim Foundation while on sabbatical leave from Harvard University Medical School. Ernst Ungewickell was supported by a grant from the Deutsche Forschungsgemeinschaft. Research was supported in part by a grant from the National Institutes of Health.

PY - 1981/11

Y1 - 1981/11

N2 - We have developed a quantitative method to study the interaction of radiolabeled clathrin triskelions with membranes from brain coated vesicles. Clathrin triskelions do not bind to coated vesicles unless these are stripped of their clathrin coat. The binding of triskelions is of high affinity (KD ≅ 2 × 10-9 M), is saturable and depends on vesicle concentration. Triskelions bind to protein-sensitive structures of the stripped vesicles. Polypeptides of about 110,000 daltons appear to be involved in the binding structure. The association of triskelions to stripped vesicles was confirmed by electron microscopy.

AB - We have developed a quantitative method to study the interaction of radiolabeled clathrin triskelions with membranes from brain coated vesicles. Clathrin triskelions do not bind to coated vesicles unless these are stripped of their clathrin coat. The binding of triskelions is of high affinity (KD ≅ 2 × 10-9 M), is saturable and depends on vesicle concentration. Triskelions bind to protein-sensitive structures of the stripped vesicles. Polypeptides of about 110,000 daltons appear to be involved in the binding structure. The association of triskelions to stripped vesicles was confirmed by electron microscopy.

UR - http://www.scopus.com/inward/record.url?scp=0019847325&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(81)90213-0

DO - 10.1016/0092-8674(81)90213-0

M3 - Article

C2 - 7034962

AN - SCOPUS:0019847325

SN - 0092-8674

VL - 26

SP - 439

EP - 446

JO - Cell

JF - Cell

IS - 3 PART 1

ER -

The binding of clathrin triskelions to membranes from coated vesicles

Abstract

Access to Document

Other files and links

Fingerprint

Cite this