Abstract
Cadherins are calcium-dependent glycoproteins that function as cell-cell adhesion molecules and are linked to the actin cytoskeleton via catenins. Newly synthesized cadherins contain a prosequence that must be proteolytically removed to generate a functional adhesion molecule. The goal of this study was to examine the proteolytic processing of N-cadherin and the assembly of the cadherin-catenin complex in cells that express endogenous N-cadherin. A monoclonal antibody specific for the proregion of human N-cadherin was generated and used to examine N-cadherin processing. Our data show that newly synthesized proN-cadherin is phosphorylated and proteolytically processed prior to transport to the plasma membrane. In addition, we show that β-catenin and plakoglobin associate only with phosphorylated proN-cadherin, whereas p120ctn can associate with both phosphorylated and non-phosphorylated proN-cadherin. Immunoprecipitations using anti-proN-cadherin showed that cadherin-catenin complexes are assembled prior to localization at the plasma membrane. These data suggest that a core N-cadherin-catenin complex assembles in the endoplasmic reticulum or Golgi compartment and is transported to the plasma membrane where linkage to the actin cytoskeleton can be established.
Original language | English (US) |
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Pages (from-to) | 17269-17276 |
Number of pages | 8 |
Journal | Journal of Biological Chemistry |
Volume | 278 |
Issue number | 19 |
DOIs | |
State | Published - May 9 2003 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology