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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Eipper, Betty A. Mains, Richard E. Duffy, Megan E. Bonnemaison, Mathilde L. Bäck, Nils Ralle, Martina |
| Description | Author Affiliation: Bonnemaison ML ( From the Departments of Molecular Biology and Biophysics and.); Bäck N ( the Department of Anatomy, Faculty of Medicine, University of Helsinki, FIN-00014 Helsinki, Finland, and.); Duffy ME ( the Department of Molecular and Medical Genetics, Oregon Health and Sciences University, Portland, Oregon 97239.); Ralle M ( the Department of Molecular and Medical Genetics, Oregon Health and Sciences University, Portland, Oregon 97239.); Mains RE ( Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030.); Eipper BA ( From the Departments of Molecular Biology and Biophysics and Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030, eipper@uchc.edu.) |
| Abstract | The adaptor protein-1 complex (AP-1), which transports cargo between the trans-Golgi network and endosomes, plays a role in the trafficking of Atp7a, a copper-transporting P-type ATPase, and peptidylglycine -amidating monooxygenase (PAM), a copper-dependent membrane enzyme. Lack of any of the four AP-1 subunits impairs function, and patients with MEDNIK syndrome, a rare genetic disorder caused by lack of expression of the σ1A subunit, exhibit clinical and biochemical signs of impaired copper homeostasis. To explore the role of AP-1 in copper homeostasis in neuroendocrine cells, we used corticotrope tumor cells in which AP-1 function was diminished by reducing expression of its µ1A subunit. Copper levels were unchanged when AP-1 function was impaired, but cellular levels of Atp7a declined slightly. The ability of PAM to function was assessed by monitoring 18-kDa fragment-NH2 production from proopiomelanocortin. Reduced AP-1 function made 18-kDa fragment amidation more sensitive to inhibition by bathocuproine disulfonate, a cell-impermeant Cu(I) chelator. The endocytic trafficking of PAM was altered, and PAM-1 accumulated on the cell surface when AP-1 levels were reduced. Reduced AP-1 function increased the Atp7a presence in early/recycling endosomes but did not alter the ability of copper to stimulate its appearance on the plasma membrane. Co-immunoprecipitation of a small fraction of PAM and Atp7a supports the suggestion that copper can be transferred directly from Atp7a to PAM, a process that can occur only when both proteins are present in the same subcellular compartment. Altered luminal cuproenzyme function may contribute to deficits observed when the AP-1 function is compromised. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-28 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adaptor Protein Complex 1 Metabolism Copper Endocytosis Mixed Function Oxygenases Multienzyme Complexes Adenosine Triphosphatases Animals Cation Transport Proteins Cell Line Cells, Cultured HeLa Cells Mice Pituitary Gland Cytology Protein Transport Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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