Complete sequence of the human mucin MUC4: a putative cell membrane-associated mucin

Author:

MONIAUX Nicolas1,NOLLET Séverine1,PORCHET Nicole12,DEGAND Pierre12,LAINE Anne1,AUBERT Jean-Pierre121

Affiliation:

1. Unité 377 INSERM, Place de Verdun, 59045 Lille Cedex, France

2. Laboratoire de Biochimie et de Biologie Moléculaire de l'Hôpital C. Huriez, 59037 Lille Cedex, France

Abstract

The MUC4 gene, which encodes a human epithelial mucin, is expressed in various epithelial tissues, just as well in adult as in poorly differentiated cells in the embryo and fetus. Its N-terminus and central sequences have previously been reported as comprising a 27-residue peptide signal, followed by a large domain varying in length from 3285 to 7285 amino acid residues. The present study establishes the whole coding sequence of MUC4 in which the C-terminus is 1156 amino acid residues long and shares a high degree of similarity with the rat sialomucin complex (SMC). SMC is a heterodimeric glycoprotein complex composed of mucin (ascites sialoglycoprotein 1, ASGP-1) and transmembrane (ASGP-2) subunits. The same organization is found in MUC4, where the presence of a GlyAspProHis proteolytic site may cleave the large precursor into two subunits, MUC4α and MUC4β. Like ASGP-2, which binds the receptor tyrosine kinase p185neu, MUC4β possesses two epidermal growth factor-like domains, a transmembrane sequence and a potential phosphorylated site. MUC4, the human homologue of rat SMC, may be a heterodimeric bifunctional cell-surface glycoprotein of 2.12 µm. These results confer a new biological role for MUC4 as a ligand for ErbB2 in cell signalling.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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