Sarah M. Carroll

Current Research:

I am interested in understanding bacterial effector proteins and how they utilize host systems during pathogenesis. I am specifically working to understand the role of SspH1, one of the effector proteins delivered into the host cell by the type 3 secretion system during Salmonella infection. SspH1 is one of several bacterial ubiquitin ligases (Rohde et al, 2007) that catalyze ubiquitination of host substrates using the the host ubiquitin machinery. SspH1 interacts with the protein PKN1 (Haraga and Miller, 2006) and inhibits the NF-KB pathway (Haraga and Miller, 2003), although it is unclear exactly how these two facets of SspH1 function are related. My main goal is to elucidate the role of SspH1 during Salmonella infection, and to understand at a mechanistic level how SspH1 is able to inhibit the NF-KB pathway. I also hope to identify new targets of this ligase and other effector proteins.

Publications:

Carroll, S.M. and Hampton, R.Y.  2010. “Usa1p is required for optimal function and regulation of the Hrd1p ER-associated degradation (ERAD) ubiquitin ligase.” J. Biol. Chem. 285:5146-5156

Yang R, Bartle S*, Otto R, Stassinopoulos A, Rogers M, Plamann L, Hartzell P. 2004. “AglZ is a filament-forming coiled-coil protein required for adventurous gliding motility of Myxococcus xanthus.” J. Bacteriol. 186(18):6168-78 *Maiden name