CHARACTERIZATION OF INTESTINALLY EXPRESSED shc-3 (K11E4.2) IN CAENORHABDITIS ELEGANS

Abstract

SHC proteins are a family of adaptor proteins that play an important role in signal transduction, they are characterized by three crucial domains: the phosphotyrosine binding (PTB) domain, a Src2 homology (SH2) domain and a less conserved collagen homolog (CH1) domain. Two Caenorhabditis elegans SHC proteins have been described: SHC-1 and SHC-2. We have identified a third SHC protein, K11E4.2, that is intestinally expressed. Our analysis revealed that K11E4.2 null mutant animals suffer from a diet-dependent change in fat accumulation and increased sensitivity to starvation and oxidative stress. C. elegans shc-1 plays a role in stress response and lifespan regulation through the insulin signaling pathway. Our data suggest that shc-1 and K11E4.2 do not act redundantly to regulate stress or starvation response, but rather each plays a distinct role in these processes. This project proposes a model where K11E4.2 could have a role as positive insulin signaling regulator in C. elegans.