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F1000Res. 2015 Dec 18;4. pii: F1000 Faculty Rev-1473. doi: 10.12688/f1000research.6866.1. eCollection 2015.

Getting to the core of cadherin complex function in Caenorhabditis elegans.

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1
Department of Zoology, University of Wisconsin-Madison, Madison, WI, USA.

Abstract

The classic cadherin-catenin complex (CCC) mediates cell-cell adhesion in metazoans. Although substantial insights have been gained by studying the CCC in vertebrate tissue culture, analyzing requirements for and regulation of the CCC in vertebrates remains challenging. Caenorhabditis elegans is a powerful system for connecting the molecular details of CCC function with functional requirements in a living organism. Recent data, using an "angstroms to embryos" approach, have elucidated functions for key residues, conserved across all metazoans, that mediate cadherin/β-catenin binding. Other recent work reveals a novel, potentially ancestral, role for the C. elegans p120ctn homologue in regulating polarization of blastomeres in the early embryo via Cdc42 and the partitioning-defective (PAR)/atypical protein kinase C (aPKC) complex. Finally, recent work suggests that the CCC is trafficked to the cell surface via the clathrin adaptor protein complex 1 (AP-1) in surprising ways. These studies continue to underscore the value of C. elegans as a model system for identifying conserved molecular mechanisms involving the CCC.

KEYWORDS:

C. elegans; Caenorhabditis elegans; cadherin; classic cadherin-catenin complex; β-catenin

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