Primate homologues of rat TGN38: primary structure, expression and functional implications

• Published in: Journal of cell science Vol. 109 ( Pt 3); no. 3; pp. 675 - 685
• Main Authors: Ponnambalam, S, Girotti, M, Yaspo, M L, Owen, C E, Perry, A C, Suganuma, T, Nilsson, T, Fried, M, Banting, G, Warren, G
• Format: Journal Article
• Language: English
• Published: England 01.03.1996
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Glycoproteins; Glycosylation; Humans; Macaca fascicularis; Male; Membrane Glycoproteins - genetics; Membrane Proteins; Molecular Sequence Data; Protein Structure, Tertiary; Repetitive Sequences, Nucleic Acid; Sequence Homology, Amino Acid
• ISSN: 0021-9533; 1477-9137
• DOI: 10.1242/jcs.109.3.675

cDNAs encoding the human and macaque homologues of rat TGN38 have been cloned and sequenced. The proteins have a highly conserved N terminus (comprising the signal peptide) and C terminus (comprising part of the lumenal domain, the membrane spanning region and cytoplasmic tail) but vary in the other part of the lumenal domain, which contains the repeat region. Whereas rat TGN38 contains 6 tandem repeats of an 8mer, both primate proteins possess 14 tandem repeats of a 14mer sequence. The human protein, like rat TGN38, is localised primarily to the TGN but is present on the cell surface and returns via endosomes. This behaviour is consistent with conservation of the membrane spanning region and the cytoplasmic tail, which contain the retention and retrieval signals, respectively, for localisation in the TGN. The unexpected differences in the lumenal domain can best be rationalised by the fact that both types of repeat domains have most of the properties of mucins. We suggest that TGN38 homologues are mucin-like molecules that regulate membrane traffic to and from the TGN.