Folding and trimerization of clathrin subunits at the triskelion hub

Inke S. Näthke; John Heuser; Andrei Lupas; Jeff Stock; Christoph W. Turck; Frances M. Brodsky

doi:10.1016/0092-8674(92)90033-9

Folding and trimerization of clathrin subunits at the triskelion hub

Inke S. Näthke, John Heuser, Andrei Lupas, Jeff Stock, Christoph W. Turck, Frances M. Brodsky

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

140 Scopus citations

Abstract

The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.

Original language	English (US)
Pages (from-to)	899-910
Number of pages	12
Journal	Cell
Volume	68
Issue number	5
DOIs	https://doi.org/10.1016/0092-8674(92)90033-9
State	Published - Mar 6 1992

All Science Journal Classification (ASJC) codes

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(92)90033-9

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title = "Folding and trimerization of clathrin subunits at the triskelion hub",

abstract = "The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.",

author = "N{\"a}thke, {Inke S.} and John Heuser and Andrei Lupas and Jeff Stock and Turck, {Christoph W.} and Brodsky, {Frances M.}",

note = "Funding Information: The dictyostelium heavy chain sequence was provided prior to publication by T. J. O{\textquoteright}Halloran and R. G.W. Anderson. This work was supported by a grant from the Pew Charitable Trusts, NIH grants GM-26691 and GM-38093 to F. Brodsky, grant GM-29647 to J. Heuser, grant Al-20980 to J. Stock, and the Howard Hughes Medical Institute to C. W. Turck.",

year = "1992",

month = mar,

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doi = "10.1016/0092-8674(92)90033-9",

language = "English (US)",

volume = "68",

pages = "899--910",

journal = "Cell",

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T1 - Folding and trimerization of clathrin subunits at the triskelion hub

AU - Näthke, Inke S.

AU - Heuser, John

AU - Lupas, Andrei

AU - Stock, Jeff

AU - Turck, Christoph W.

AU - Brodsky, Frances M.

N1 - Funding Information: The dictyostelium heavy chain sequence was provided prior to publication by T. J. O’Halloran and R. G.W. Anderson. This work was supported by a grant from the Pew Charitable Trusts, NIH grants GM-26691 and GM-38093 to F. Brodsky, grant GM-29647 to J. Heuser, grant Al-20980 to J. Stock, and the Howard Hughes Medical Institute to C. W. Turck.

PY - 1992/3/6

Y1 - 1992/3/6

N2 - The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.

AB - The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.

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U2 - 10.1016/0092-8674(92)90033-9

DO - 10.1016/0092-8674(92)90033-9

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AN - SCOPUS:0026503136

SN - 0092-8674

VL - 68

SP - 899

EP - 910

JO - Cell

JF - Cell

IS - 5

ER -

Folding and trimerization of clathrin subunits at the triskelion hub

Abstract

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