Generation of ligand-receptor alliances by "SEA" module-mediated cleavage of membrane-associated mucin proteins.
Ontology highlight
ABSTRACT: A mechanism is described whereby one and the same gene can encode both a receptor protein as well as its specific ligand. Generation of this receptor-ligand partnership is effected by proteolytic cleavage within a specific module located in a membrane resident protein. It is postulated here that the "SEA" module, found in a number of heavily O-linked glycosylated membrane-associated proteins, serves as a site for proteolytic cleavage. The subunits generated by proteolytic cleavage of the SEA module reassociate, and can subsequently elicit a signaling cascade. We hypothesize that all membrane resident proteins containing such a "SEA" module will undergo cleavage, thereby generating a receptor-ligand alliance. This requires that the protein subunits resulting from the proteolytic cleavage re
SUBMITTER: Wreschner DH
PROVIDER: S-EPMC2373471 | biostudies-literature | 2002 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA