Jean-Paul Borg — Page 2

PubMed2002

The LAP family: a phylogenetic point of view.

Recently, the LAP (for 'LRR and PDZ') family of adaptor proteins was described in vertebrates and invertebrates. The proteins are involved in cell polarity and receptor targeting, and they contain both LRR and PDZ domains in the same molecule, a combination that is specifically bilaterian. A search of available genome sequences reveals a limited number of lap genes, which we have classified by phylogenetic analysis. We propose a functional hypothesis for the origin of this protein family in bilaterians, and give a phylogenetic interpretation of their diversity.

Amino Acid Sequence↗

PubMed2001

Interaction between Erbin and a Catenin-related protein in epithelial cells.

Integrity of epithelial tissues relies on the proper apical-basolateral polarity of epithelial cells. Members of the LAP (LRR and PDZ) protein family such as LET-413 and Scribble are involved in maintaining epithelial cell polarity in Caenorhabditis elegans and Drosophila melanogaster, respectively. We previously described Erbin as a mammalian LET-413 homologue interacting with ERBB2/HER2, an epidermal growth factor receptor family member. Erbin and ERBB2/HER2 are located in the basolateral membranes of epithelial cells. We show here that Erbin interacts with p0071 (also called plakophilin-4), an armadillo repeat protein linked to the cytoskeleton. Erbin binds to p0071 in vitro and in vivo in a PDZ domain-dependent manner, and both proteins colocalized in desmosomes of epithelial cells. Using a dominant negative approach, we found that integrity of epithelial cell monolayer is impaired when interaction between Erbin and p0071 is disrupted. We propose that Erbin is connected by p0071 to cytoskeletal networks in an interaction crucial for epithelial homeostasis.

Adaptor Proteins, Signal Transducing↗