Endolyn is a mucin-like type I membrane protein targeted to lysosomes by its cytoplasmic tail
Autor: | G, Ihrke, S R, Gray, J P, Luzio |
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Rok vydání: | 2000 |
Předmět: |
Membrane Glycoproteins
Base Sequence Sequence Homology Amino Acid Recombinant Fusion Proteins Molecular Sequence Data Mucins Cell Polarity Lysosome-Associated Membrane Glycoproteins Receptors Cell Surface CD146 Antigen Sequence Analysis DNA Protein Sorting Signals Endolyn Cell Compartmentation Rats Liver Antigens CD Animals Amino Acid Sequence Disulfides Lysosomes Neural Cell Adhesion Molecules Conserved Sequence Gene Library Research Article |
Zdroj: | The Biochemical journal. |
ISSN: | 0264-6021 |
Popis: | Endolyn (endolyn-78) is a membrane protein found in lysosomal and endosomal compartments of mammalian cells. Unlike 'classical' lysosomal membrane proteins, such as lysosome-associated membrane protein (lamp)-1, it is also present in a subapical compartment in polarized WIF-B hepatocytes. The structural features that determine sorting of endolyn are unknown. We have identified a rat endolyn cDNA by expression screening. The cDNA encodes a ubiquitously expressed type I membrane protein with a short cytoplasmic tail of 13 amino acids and many putative sites for N- and O-linked glycosylation in the predicted luminal domain. Endolyn is closely related to two human mucin-like proteins, multi-glycosylated core protein (MGC)-24 and CD164 (MGC-24v), expressed in gastric carcinoma cells and bone marrow stromal and haematopoietic precursor cells respectively. The predicted transmembrane and cytoplasmic tail domains of endolyn, as well as parts of its luminal domain, also show some similarities with lamp-1 and lamp-2. Like these and other known lysosomal membrane proteins, endolyn contains a YXXO motif at the C-terminus of its cytoplasmic tail (where O is a bulky hydrophobic amino acid), but with no preceding glycine. Nonetheless, the last ten amino acids of this tail, when transplanted on to human CD8, caused efficient targeting of the chimaeric protein to endosomes and lysosomes in transfected normal rat kidney cells. |
Databáze: | OpenAIRE |
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