The endoplasmic reticulum-associated protein degradation (ERAD) pathway serves as a “quality control” mechanism for proteins destined for secretion outside of the cell. If a secretory protein fails to adopt the correct functional structure, molecules of the ERAD network will direct the misfolded protein to the proteasome, where it is broken down. ERAD malfunction has been implicated in a variety of diseases, including Parkinson’s, cystic fibrosis, and HIV. The human proteins CGI-112 and COX4NB have recently been identified as components of the ERAD network. These proteins exhibit a sequence similarity of 40%; both proteins have been shown to bind to TTC35, a subunit of the ER membrane protein complex. In order to gain an understanding of the intermolecular interactions that modulate ERAD activity, we produced template-based structural models of the former two proteins. The models indicate significant structural differences in the C-terminal domain. This study compares the <i>in vitro</i> binding characteristics of CGI-112, COX4NB, and the CGI-112 C-terminal domain.

Characterization of the C-terminal domain of CGI-112, a protein involved in the ER-associated degradation pathway

249th National Meeting (2015)

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