gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer
| Autor: | Jean-Pierre Paccaud, Michel Dominguez, Ali Fazel, Kurt Dejgaard, David Y. Thomas, Joachim Füllekrug, Sophie Dahan, John J.M. Bergeron, Tommy Nilsson |
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| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
DNA
Complementary Saccharomyces cerevisiae Proteins Protein family Molecular Sequence Data Vesicular Transport Proteins Fluorescent Antibody Technique Golgi Apparatus Endocytosis Coatomer Protein Article HeLa Cytosol Animals Frozen Sections Humans pharmaceutical Amino Acid Sequence Cis-Golgi network Cloning Molecular Binding Sites biology Base Sequence Sequence Homology Amino Acid Membrane Proteins Cell Biology COPI biology.organism_classification Molecular biology In vitro Rats Microscopy Electron Liver Cytoplasm Coatomer Carrier Proteins HeLa Cells Protein Binding Subcellular Fractions |
| Zdroj: | The Journal of Cell Biology |
| Popis: | Five mammalian members of the gp25L/ emp24/p24 family have been identified as major constituents of the cis-Golgi network of rat liver and HeLa cells. Two of these were also found in membranes of higher density (corresponding to the ER), and this correlated with their ability to bind COP I in vitro. This binding was mediated by a K(X)KXX-like retrieval motif present in the cytoplasmic domain of these two members. A second motif, double phenylalanine (FF), present in the cytoplasmic domain of all five members, was shown to participate in the binding of Sec23 (COP II). This motif is part of a larger one, similar to the F/YXXXXF/Y strong endocytosis and putative AP2 binding motif. In vivo mutational analysis confirmed the roles of both motifs so that when COP I binding was expected to be impaired, cell surface expression was observed, whereas mutation of the Sec23 binding motif resulted in a redistribution to the ER. Surprisingly, upon expression of mutated members, steady-state distribution of unmutated ones shifted as well, presumably as a consequence of their observed oligomeric properties. |
| Databáze: | OpenAIRE |
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