Positively charged cytoplasmic residues in corin prevent signal peptidase cleavage and endoplasmic reticulum retention.

ABSTRACT: Positively charged residues are commonly located near the cytoplasm-membrane interface, which is known as the positive-inside rule in membrane topology. The mechanism underlying the function of these charged residues remains poorly understood. Herein, we studied the function of cytoplasmic residues in corin, a type II transmembrane serine protease in cardiovascular biology. We found that the positively charged residue at the cytoplasm-membrane interface of corin was not a primary determinant in membrane topology but probably served as a charge-repulsion mechanism in the endoplasmic reticulum (ER) to prevent interactions with proteins in the ER, including the signal peptidase. Substitution of the positively charged residue with a neutral or acidic residue resulted in corin secretion likely

SUBMITTER: Li H 

PROVIDER: S-EPMC11756421 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature