Deconstructing the cadherin-catenin-actin complex

Soichiro Yamada, Sabine Pokutta, Frauke Drees, William I. Weis, W. James Nelson

Research output: Contribution to journalArticle

700 Citations (Scopus)

Abstract

Spatial and functional organization of cells in tissues is determined by cell-cell adhesion, thought to be initiated through trans-interactions between extracellular domains of the cadherin family of adhesion proteins, and strengthened by linkage to the actin cytoskeleton. Prevailing dogma is that cadherins are linked to the actin cytoskeleton through β-catenin and α-catenin, although the quaternary complex has never been demonstrated. We test this hypothesis and find that α-catenin does not interact with actin filaments and the E-cadherin-β-catenin complex simultaneously, even in the presence of the actin binding proteins vinculin and α-actinin, either in solution or on isolated cadherin-containing membranes. Direct analysis in polarized cells shows that mobilities of E-cadherin, β-catenin, and α-catenin are similar, regardless of the dynamic state of actin assembly, whereas actin and several actin binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously appreciated.

Original languageEnglish (US)
Pages (from-to)889-901
Number of pages13
JournalCell
Volume123
Issue number5
DOIs
StatePublished - Dec 2 2005
Externally publishedYes

Fingerprint

Catenins
Cadherins
Actins
Actin Cytoskeleton
Microfilament Proteins
Vinculin
Actinin
Cell adhesion
Cell Adhesion
Adhesion
Tissue
Membranes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Yamada, S., Pokutta, S., Drees, F., Weis, W. I., & Nelson, W. J. (2005). Deconstructing the cadherin-catenin-actin complex. Cell, 123(5), 889-901. https://doi.org/10.1016/j.cell.2005.09.020

Deconstructing the cadherin-catenin-actin complex. / Yamada, Soichiro; Pokutta, Sabine; Drees, Frauke; Weis, William I.; Nelson, W. James.

In: Cell, Vol. 123, No. 5, 02.12.2005, p. 889-901.

Research output: Contribution to journalArticle

Yamada, S, Pokutta, S, Drees, F, Weis, WI & Nelson, WJ 2005, 'Deconstructing the cadherin-catenin-actin complex', Cell, vol. 123, no. 5, pp. 889-901. https://doi.org/10.1016/j.cell.2005.09.020
Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ. Deconstructing the cadherin-catenin-actin complex. Cell. 2005 Dec 2;123(5):889-901. https://doi.org/10.1016/j.cell.2005.09.020
Yamada, Soichiro ; Pokutta, Sabine ; Drees, Frauke ; Weis, William I. ; Nelson, W. James. / Deconstructing the cadherin-catenin-actin complex. In: Cell. 2005 ; Vol. 123, No. 5. pp. 889-901.
@article{49413e4c37df450486f2f5af0094226d,
title = "Deconstructing the cadherin-catenin-actin complex",
abstract = "Spatial and functional organization of cells in tissues is determined by cell-cell adhesion, thought to be initiated through trans-interactions between extracellular domains of the cadherin family of adhesion proteins, and strengthened by linkage to the actin cytoskeleton. Prevailing dogma is that cadherins are linked to the actin cytoskeleton through β-catenin and α-catenin, although the quaternary complex has never been demonstrated. We test this hypothesis and find that α-catenin does not interact with actin filaments and the E-cadherin-β-catenin complex simultaneously, even in the presence of the actin binding proteins vinculin and α-actinin, either in solution or on isolated cadherin-containing membranes. Direct analysis in polarized cells shows that mobilities of E-cadherin, β-catenin, and α-catenin are similar, regardless of the dynamic state of actin assembly, whereas actin and several actin binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously appreciated.",
author = "Soichiro Yamada and Sabine Pokutta and Frauke Drees and Weis, {William I.} and Nelson, {W. James}",
year = "2005",
month = "12",
day = "2",
doi = "10.1016/j.cell.2005.09.020",
language = "English (US)",
volume = "123",
pages = "889--901",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - Deconstructing the cadherin-catenin-actin complex

AU - Yamada, Soichiro

AU - Pokutta, Sabine

AU - Drees, Frauke

AU - Weis, William I.

AU - Nelson, W. James

PY - 2005/12/2

Y1 - 2005/12/2

N2 - Spatial and functional organization of cells in tissues is determined by cell-cell adhesion, thought to be initiated through trans-interactions between extracellular domains of the cadherin family of adhesion proteins, and strengthened by linkage to the actin cytoskeleton. Prevailing dogma is that cadherins are linked to the actin cytoskeleton through β-catenin and α-catenin, although the quaternary complex has never been demonstrated. We test this hypothesis and find that α-catenin does not interact with actin filaments and the E-cadherin-β-catenin complex simultaneously, even in the presence of the actin binding proteins vinculin and α-actinin, either in solution or on isolated cadherin-containing membranes. Direct analysis in polarized cells shows that mobilities of E-cadherin, β-catenin, and α-catenin are similar, regardless of the dynamic state of actin assembly, whereas actin and several actin binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously appreciated.

AB - Spatial and functional organization of cells in tissues is determined by cell-cell adhesion, thought to be initiated through trans-interactions between extracellular domains of the cadherin family of adhesion proteins, and strengthened by linkage to the actin cytoskeleton. Prevailing dogma is that cadherins are linked to the actin cytoskeleton through β-catenin and α-catenin, although the quaternary complex has never been demonstrated. We test this hypothesis and find that α-catenin does not interact with actin filaments and the E-cadherin-β-catenin complex simultaneously, even in the presence of the actin binding proteins vinculin and α-actinin, either in solution or on isolated cadherin-containing membranes. Direct analysis in polarized cells shows that mobilities of E-cadherin, β-catenin, and α-catenin are similar, regardless of the dynamic state of actin assembly, whereas actin and several actin binding proteins have higher mobilities. These results suggest that the linkage between the cadherin-catenin complex and actin filaments is more dynamic than previously appreciated.

UR - http://www.scopus.com/inward/record.url?scp=28344433073&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=28344433073&partnerID=8YFLogxK

U2 - 10.1016/j.cell.2005.09.020

DO - 10.1016/j.cell.2005.09.020

M3 - Article

VL - 123

SP - 889

EP - 901

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

ER -