Surface structure of the COPII-coated vesicle

Ken Matsuoka, Randy Schekman, Lelio Orci, John E. Heuser

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

The spatial arrangement of COPII coat protein subunits was analyzed by crosslinking to an artificial membrane surface and by electron microscopy of coat proteins and coated vesicle surfaces. The efficiency of COPII subunit crosslinking to phospholipids declined in order of protein recruitment to the coat: Sar1p > Sec23/24p ≫ Sec13/31p. Deep-etch rotary shadowing and electron microscopy were used to explore the COPII subunit structure with isolated proteins and coated vesicles. Sec23/24 resembles a bow tie, and Sec13/31p contains terminal bilobed globular structures bordering a central rod. The surface structure of COPII vesicles revealed a coat built with polygonal units. The length of the side of the hexagonal/pentagonal units is close to the dimension of the central rod-like segment of Sec13/31. Partially uncoated profiles revealed strands of Sec13/31p stripped from the vesicle surface. We conclude that the coat subunits form layers displaced from the membrane surface in reverse order of addition to the coat.

Original languageEnglish
Pages (from-to)13705-13709
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number24
DOIs
Publication statusPublished - Nov 20 2001
Externally publishedYes

Fingerprint

COP-Coated Vesicles
Coated Vesicles
Capsid Proteins
Electron Microscopy
Artificial Membranes
Protein Subunits
Phospholipids
Proteins
Membranes

All Science Journal Classification (ASJC) codes

  • Genetics
  • General

Cite this

Surface structure of the COPII-coated vesicle. / Matsuoka, Ken; Schekman, Randy; Orci, Lelio; Heuser, John E.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 98, No. 24, 20.11.2001, p. 13705-13709.

Research output: Contribution to journalArticle

Matsuoka, Ken ; Schekman, Randy ; Orci, Lelio ; Heuser, John E. / Surface structure of the COPII-coated vesicle. In: Proceedings of the National Academy of Sciences of the United States of America. 2001 ; Vol. 98, No. 24. pp. 13705-13709.
@article{edd25c03b2b0459ebc39b903cd5ff3b2,
title = "Surface structure of the COPII-coated vesicle",
abstract = "The spatial arrangement of COPII coat protein subunits was analyzed by crosslinking to an artificial membrane surface and by electron microscopy of coat proteins and coated vesicle surfaces. The efficiency of COPII subunit crosslinking to phospholipids declined in order of protein recruitment to the coat: Sar1p > Sec23/24p ≫ Sec13/31p. Deep-etch rotary shadowing and electron microscopy were used to explore the COPII subunit structure with isolated proteins and coated vesicles. Sec23/24 resembles a bow tie, and Sec13/31p contains terminal bilobed globular structures bordering a central rod. The surface structure of COPII vesicles revealed a coat built with polygonal units. The length of the side of the hexagonal/pentagonal units is close to the dimension of the central rod-like segment of Sec13/31. Partially uncoated profiles revealed strands of Sec13/31p stripped from the vesicle surface. We conclude that the coat subunits form layers displaced from the membrane surface in reverse order of addition to the coat.",
author = "Ken Matsuoka and Randy Schekman and Lelio Orci and Heuser, {John E.}",
year = "2001",
month = "11",
day = "20",
doi = "10.1073/pnas.241522198",
language = "English",
volume = "98",
pages = "13705--13709",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "24",

}

TY - JOUR

T1 - Surface structure of the COPII-coated vesicle

AU - Matsuoka, Ken

AU - Schekman, Randy

AU - Orci, Lelio

AU - Heuser, John E.

PY - 2001/11/20

Y1 - 2001/11/20

N2 - The spatial arrangement of COPII coat protein subunits was analyzed by crosslinking to an artificial membrane surface and by electron microscopy of coat proteins and coated vesicle surfaces. The efficiency of COPII subunit crosslinking to phospholipids declined in order of protein recruitment to the coat: Sar1p > Sec23/24p ≫ Sec13/31p. Deep-etch rotary shadowing and electron microscopy were used to explore the COPII subunit structure with isolated proteins and coated vesicles. Sec23/24 resembles a bow tie, and Sec13/31p contains terminal bilobed globular structures bordering a central rod. The surface structure of COPII vesicles revealed a coat built with polygonal units. The length of the side of the hexagonal/pentagonal units is close to the dimension of the central rod-like segment of Sec13/31. Partially uncoated profiles revealed strands of Sec13/31p stripped from the vesicle surface. We conclude that the coat subunits form layers displaced from the membrane surface in reverse order of addition to the coat.

AB - The spatial arrangement of COPII coat protein subunits was analyzed by crosslinking to an artificial membrane surface and by electron microscopy of coat proteins and coated vesicle surfaces. The efficiency of COPII subunit crosslinking to phospholipids declined in order of protein recruitment to the coat: Sar1p > Sec23/24p ≫ Sec13/31p. Deep-etch rotary shadowing and electron microscopy were used to explore the COPII subunit structure with isolated proteins and coated vesicles. Sec23/24 resembles a bow tie, and Sec13/31p contains terminal bilobed globular structures bordering a central rod. The surface structure of COPII vesicles revealed a coat built with polygonal units. The length of the side of the hexagonal/pentagonal units is close to the dimension of the central rod-like segment of Sec13/31. Partially uncoated profiles revealed strands of Sec13/31p stripped from the vesicle surface. We conclude that the coat subunits form layers displaced from the membrane surface in reverse order of addition to the coat.

UR - http://www.scopus.com/inward/record.url?scp=0035923641&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035923641&partnerID=8YFLogxK

U2 - 10.1073/pnas.241522198

DO - 10.1073/pnas.241522198

M3 - Article

VL - 98

SP - 13705

EP - 13709

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 24

ER -