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 journalArticlepeer-review

26 Scopus citations


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
Issue number4
StatePublished - 2008


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

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology


Dive into the research topics of 'E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/golgi compartments'. Together they form a unique fingerprint.

Cite this