T-cadherin GPI-anchor is insufficient for apical targeting in MDCK cells. Academic Article uri icon

Overview

abstract

  • T-cadherin is a 95kDa glycoprotein member of the cadherin family of adhesion molecules attached to the extracellular surface of the cell membrane through a glycosyl-phosphatidylinositol (GPI)-anchor. Whether a T-cadherin ectodomain apical targeting signal or the GPI-anchor itself targets this protein to the apical membrane is not known. Chimeras of the reporter EGFP and T-cadherin have demonstrated that a minimal construct consisting of the C-terminal 25 amino acids including the N690 (omega-site) of T-cadherin was sufficient to GPI-anchor the EGFP protein. However, efficient GPI-anchor with minimal secretion of the protein required an additional 5 residues (omega-1 to omega-5). The GPI-anchored chimeras fractionated to the Triton X-100 detergent insoluble fraction and were released to the cell culture supernatant by phosphoinositide-specific phospho-lipase C digestion. When expressed in MDCK cells, all GPI-anchored chimeras targeted to the basolateral membrane, while the T/N-chimera and the wild-type T-cadherin targeted to the apical membrane. Therefore, T-cadherin is an example of another rare GPI-anchored protein where the anchor itself is not sufficient for apical targeting in MDCK cells.

publication date

  • April 8, 2005

Research

keywords

  • Cadherins
  • Glycosylphosphatidylinositols
  • Kidney
  • Protein Transport

Identity

Scopus Document Identifier

  • 14644399253

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2005.02.020

PubMed ID

  • 15737631

Additional Document Info

volume

  • 329

issue

  • 2