KDEL proteins are found on the surface of NG108-15 cells
| Autor: | Richard E. Fine, Hae Yung Pyun, Guangqing Xiao, Robin J. Johnson, Tzu-Feng Chung |
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| Rok vydání: | 1999 |
| Předmět: |
Receptors
Peptide Glucose-regulated protein KDEL Protein Disulfide-Isomerases Biology Endoplasmic Reticulum Cellular and Molecular Neuroscience Mice Neuroblastoma Protein structure Calnexin Neurites Tumor Cells Cultured Animals Biotinylation Amino Acid Sequence Protein disulfide-isomerase Molecular Biology Endoplasmic Reticulum Chaperone BiP Heat-Shock Proteins Neurons Brefeldin A Endoplasmic reticulum Calcium-Binding Proteins Antibodies Monoclonal Membrane Proteins Biological Transport Transmembrane protein Cell biology Neoplasm Proteins Protein Structure Tertiary Bucladesine Ribonucleoproteins biology.protein Calreticulin Carrier Proteins Molecular Chaperones |
| Zdroj: | Brain research. Molecular brain research. 72(2) |
| ISSN: | 0169-328X |
| Popis: | Although KDEL proteins are primarily localized to the endoplasmic reticulum (ER), we have employed surface biotinylation method to demonstrate that the KDEL proteins calreticulin (Crt), protein disulfide isomerase (PDI) and the 78-kDa glucose regulated protein (GRP78) are found on the surface of the NG108-15 cell line. In contrast, the 94-kDa glucose regulated protein (GRP94), another KDEL protein, is not found on the cell surface. Calnexin (Cnx), a type-1 integral transmembrane ER protein which is partially homologous to Crt but lacks the KDEL sequence, is not detected on the cell surface either. While only small amounts of the total GRP78, PDI and Crt molecules exist on the cell surface at steady state, a significant fraction of the newly synthesized molecules are transported to the cell surface and transport of these proteins is inhibited by treatment with brefeldin A. The surface GRP78 contains the KDEL sequence. On the cell surface, GRP78, PDI and Crt associate with other proteins and form complexes of different sizes. Surface Crt is found to be essential for the neurite formation when NG108-15 cells are induced to differentiate using dibutyryl cAMP. |
| Databáze: | OpenAIRE |
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