Functional relevance of a novel SlyX motif in non-conventional secretion of insulin-degrading enzyme.

ABSTRACT: Insulin-degrading enzyme (IDE) is a Zn(2+) metalloprotease with a characteristic inverted catalytic motif. IDE is ubiquitously expressed and degrades peptide substrates including insulin, endorphin, and the amyloid-β peptide. Although IDE is mainly expressed in the cytosol, it can also be found on the cell surface and in secreted form in extracellular fluids. As IDE lacks a characteristic signal sequence that targets the protein to the classical secretory pathway, release of the enzyme involves non-conventional mechanisms. However, functional domains of IDE involved in its secretion remain elusive. By bioinformatical, biochemical, and cell biological methods, we identified a novel amino acid motif ((853)EKPPHY(858)) close to the C terminus of IDE and characterized its function in the non-c

SUBMITTER: Glebov K 

PROVIDER: S-EPMC3123038 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature