Rainer Prohaska Lab

Molecular cell biology and structure of the lipid raft proteins stomatin and stomatin-like protein 1
 
Our group investigates the structure and function of stomatin and stomatin-like protein 1 (SLP-1), two integral proteins that are anchored at the cytoplasmic side of the membrane via a hydrophobic domain and palmitoylation and contain an SPFH (stomatin, prohibitin, flotillin, HflK/C) domain that is also bound to the membrane. Stomatin is an oligomeric protein, associated with lipid microdomains, known as lipid rafts, and is thought to act as a scaffolding protein like caveolin-1. It is a major protein of the red blood cell membrane but is also widely expressed in most tissues and found in animals, plants and prokaryotes.
 
SLP-1 is mainly expressed in brain and skeletal muscle. Its homologue in C. elegans, UNC-24, plays an essential role in motor neurons. Due to an SCP-2 (sterol carrier protein 2) domain, SLP-1 is thought to act as a membrane-bound lipid transfer protein.