Proteins with multiple membrane-segments (MS) initially insert into the endoplasmic reticulum (ER) of eukaryotic cells. Little is known how such proteins attain native functional structures. We study the ER membrane chaperone Shr3 that specifically facilitates the folding of all 18 members of the yeast amino acid permease family of proteins with 12 MS.
Amino acids are essential nutrients that serve as building blocks of proteins and some are efficiently metabolized for energy. Eukaryotic cells respond to extracellular amino acids by enhancing their uptake. We study the molecular mechanisms underlying this response and the role of amino acid metabolism in promoting virulent growth of human fungal pathogens.
