Polymorphisms in DLGH1 and LAMC1 in Mayer–Rokitansky–Kuster–Hauser syndrome  Celia Ravel, Anu Bashamboo, Joelle Bignon-Topalovic, Jean-Pierre Siffroi, Ken McElreavey, Emile Darai  Reproductive BioMedicine Online  Volume 24, Issue 4, Pages 462-465 (April 2012) DOI: 10.1016/j.rbmo.2011.12.008 Copyright © 2012 Reproductive Healthcare Ltd. Terms and Conditions

Figure 1 DLGH1 (discs, large homologue 1, Drosophilia) and LAMC1 (laminin gamma 1) signal cascades. In epithelial cells, DLGH1 is located at the membrane–cytoskeleton interface and is associated with E-cadherin and also binds to adenomatous polyposis coli (APC) tumour suppressor protein. Classical cadherins have cytoplasmic domains that bind α-, β- and γ-catenin. These complexes link actin microfilaments, allowing the organization of the actin cytoskeleton at junctional complexes, the establishment of membrane domains, and the modulation of signal transduction pathways. LAMC1 is one of the three chains composing laminins, a family of extracellular matrix glycoproteins that constitute basement membranes. They are involved in a wide variety of biological processes including cell adhesion, differentiation, migration and signalling in the epithelial cell. It binds to extracellular domains of the integrin transmembrane receptors, which are heterodimeric molecules composed of α and β subunits. These have cytoplasmic domains, which associate with the actin cytoskeleton, affiliated proteins and signalling molecules including focal adhesion kinase (FAK) and talin. Together, both proteins, DLGH1 and LAMC1, may be crucial for the cell by stabilizing cytoskeletal attachment or remodelling. Reproductive BioMedicine Online 2012 24, 462-465DOI: (10.1016/j.rbmo.2011.12.008) Copyright © 2012 Reproductive Healthcare Ltd. Terms and Conditions