E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/golgi compartments

Matthew W. Curtis, Keith R Johnson, Margaret J. Wheelock

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.

Original languageEnglish (US)
Pages (from-to)365-378
Number of pages14
JournalCell Communication and Adhesion
Volume15
Issue number4
DOIs
StatePublished - Nov 11 2008

Fingerprint

Catenins
Cadherins
Endoplasmic Reticulum
Protein Sorting Signals
Adhesion
Antibodies

Keywords

  • Adhesion
  • Catenin
  • E-cadherin
  • Golgi complex
  • N-cadherin
  • Prosequence

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology

Cite this

E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/golgi compartments. / Curtis, Matthew W.; Johnson, Keith R; Wheelock, Margaret J.

In: Cell Communication and Adhesion, Vol. 15, No. 4, 11.11.2008, p. 365-378.

Research output: Contribution to journalArticle

@article{0f521562ecd04b30a27651c7a08ff0c2,
title = "E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/golgi compartments",
abstract = "Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.",
keywords = "Adhesion, Catenin, E-cadherin, Golgi complex, N-cadherin, Prosequence",
author = "Curtis, {Matthew W.} and Johnson, {Keith R} and Wheelock, {Margaret J.}",
year = "2008",
month = "11",
day = "11",
doi = "10.1080/15419060802460748",
language = "English (US)",
volume = "15",
pages = "365--378",
journal = "Cell Adhesion and Communication",
issn = "1541-9061",
publisher = "Informa Healthcare",
number = "4",

}

TY - JOUR

T1 - E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/golgi compartments

AU - Curtis, Matthew W.

AU - Johnson, Keith R

AU - Wheelock, Margaret J.

PY - 2008/11/11

Y1 - 2008/11/11

N2 - Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.

AB - Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.

KW - Adhesion

KW - Catenin

KW - E-cadherin

KW - Golgi complex

KW - N-cadherin

KW - Prosequence

UR - http://www.scopus.com/inward/record.url?scp=55449109862&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=55449109862&partnerID=8YFLogxK

U2 - 10.1080/15419060802460748

DO - 10.1080/15419060802460748

M3 - Article

C2 - 18937087

AN - SCOPUS:55449109862

VL - 15

SP - 365

EP - 378

JO - Cell Adhesion and Communication

JF - Cell Adhesion and Communication

SN - 1541-9061

IS - 4

ER -