Mechanism of caveolin filament assembly

Imma Fernandez, Yunshu Ying, Joseph Albanesi, Richard G W Anderson

Research output: Contribution to journalArticle

108 Citations (Scopus)

Abstract

Caveolin-1 was the first protein identified that colocalizes with the ≈10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cav1-101) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an α-helix. Cav1-101 oligomers are ≈11 nm in diameter and contain seven molecules of Cav1-101. These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the α-helices of the seven Cav1-101 units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.

Original languageEnglish (US)
Pages (from-to)11193-11198
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number17
DOIs
StatePublished - Aug 20 2002

Fingerprint

Caveolins
Caveolin 1
Caveolae
Ultracentrifugation
Circular Dichroism
Electron Microscopy
Amino Acids
Membranes
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Mechanism of caveolin filament assembly. / Fernandez, Imma; Ying, Yunshu; Albanesi, Joseph; Anderson, Richard G W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, No. 17, 20.08.2002, p. 11193-11198.

Research output: Contribution to journalArticle

Fernandez, Imma ; Ying, Yunshu ; Albanesi, Joseph ; Anderson, Richard G W. / Mechanism of caveolin filament assembly. In: Proceedings of the National Academy of Sciences of the United States of America. 2002 ; Vol. 99, No. 17. pp. 11193-11198.
@article{88cf1e1a8d5f481f8f22da608a26099c,
title = "Mechanism of caveolin filament assembly",
abstract = "Caveolin-1 was the first protein identified that colocalizes with the ≈10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cav1-101) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an α-helix. Cav1-101 oligomers are ≈11 nm in diameter and contain seven molecules of Cav1-101. These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the α-helices of the seven Cav1-101 units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.",
author = "Imma Fernandez and Yunshu Ying and Joseph Albanesi and Anderson, {Richard G W}",
year = "2002",
month = "8",
day = "20",
doi = "10.1073/pnas.172196599",
language = "English (US)",
volume = "99",
pages = "11193--11198",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "17",

}

TY - JOUR

T1 - Mechanism of caveolin filament assembly

AU - Fernandez, Imma

AU - Ying, Yunshu

AU - Albanesi, Joseph

AU - Anderson, Richard G W

PY - 2002/8/20

Y1 - 2002/8/20

N2 - Caveolin-1 was the first protein identified that colocalizes with the ≈10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cav1-101) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an α-helix. Cav1-101 oligomers are ≈11 nm in diameter and contain seven molecules of Cav1-101. These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the α-helices of the seven Cav1-101 units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.

AB - Caveolin-1 was the first protein identified that colocalizes with the ≈10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cav1-101) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an α-helix. Cav1-101 oligomers are ≈11 nm in diameter and contain seven molecules of Cav1-101. These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the α-helices of the seven Cav1-101 units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.

UR - http://www.scopus.com/inward/record.url?scp=0037143666&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037143666&partnerID=8YFLogxK

U2 - 10.1073/pnas.172196599

DO - 10.1073/pnas.172196599

M3 - Article

VL - 99

SP - 11193

EP - 11198

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 - 17

ER -