title: Membrane topology of the C. elegans SEL-12 presenilin.
abstract: Mutant presenilins cause Alzheimer's disease. Presenilins have multiple hydrophobic regions that could theoretically span a membrane, and a knowledge of the membrane topology is crucial for deducing the mechanism of presenilin function. By analyzing the activity of beta-galactosidase hybrid proteins expressed in C. elegans, we show that the C. elegans SEL-12 presenilin has eight transmembrane domains and that there is a cleavage site after the sixth transmembrane domain. We examine the presenilin sequence in view of the predicted topology and discuss possible mechanisms for presenilin function.
authors.affiliation: Integrated Program in Cellular, Molecular, and Biophysical Studies, Columbia University, College of Physicians and Surgeons, New York, New York 10032, USA.
authors.forename: X
authors.initials: X
authors.lastname: Li
authors.forename: I
authors.initials: I
authors.lastname: Greenwald
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics*; D029742:Caenorhabditis elegans Proteins; D003600:Cytosol / Q000737:chemistry; D005260:Female; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D053764:Presenilin-1; D053766:Presenilin-2; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D019076:Transgenes
chemical_list: D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; D008565:Membrane Proteins; D053764:Presenilin-1; D053766:Presenilin-2; C095907:SEL-12 protein, C elegans