Molecular Signaling in Collagen Proteins

An article in the American Journal of Human Genetics describes the importance of COL4A2 for the secretion of COL4A1 and the normal function of both proteins [1].

The most surprising finding is that all mutations are not glycin mutations as in most collagen related disorders. The mutations are in fact missense mutations in the collageneous domain that affect highly conserved amino acids. This finding indicates molecular signals that have to be discovered.

From fauceir perspective this example demonstrates the nested structure and modularity of fauceirs. Thus an amino acid chain conteins signaling structure that participate in other fauceir's control loops. These mutations not only affect the secretion of the protein itself, but also the secretion of its cousin protein coded by the COL4A1 gene.

1. Marion Jeanne u. a., „COL4A2 Mutations Impair COL4A1 and COL4A2 Secretion and Cause Hemorrhagic Stroke“, American Journal of Human Genetics (Dezember 29, 2011), http://www.ncbi.nlm.nih.gov/pubmed/22209247.