Protein interacting with Amyloid Precursor Protein tail-1 (PAT1) is involved in early endocytosis
| Autor: | Léa Huguet, Lidia Tagliafierro, Stéphanie Chasseigneaux, David Geny, Fabian Corlier, Marie-Claude Potier, Vincent Contremoulins, Florian Rebeillard, Lucie Gorisse-Hussonnois, Michèle Darmon, Aysegul Dilsizoglu Senol, Bernadette Allinquant |
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| Rok vydání: | 2019 |
| Předmět: |
Amino Acid Transport Systems
Vesicular Transport Proteins Transferrin receptor Endosomes Endocytosis EEA1 Amyloid beta-Protein Precursor Mice 03 medical and health sciences Cellular and Molecular Neuroscience Amyloid precursor protein Animals Humans Molecular Biology rab5 GTP-Binding Proteins Neurons Pharmacology chemistry.chemical_classification 0303 health sciences Symporters biology rab4 GTP-Binding Proteins Chemistry Vesicle Cell Membrane fungi 030302 biochemistry & molecular biology rab7 GTP-Binding Proteins Cell Biology Cell biology Androgen receptor Protein Transport Gene Expression Regulation Receptors Androgen rab GTP-Binding Proteins Transferrin biology.protein Molecular Medicine Binding domain |
| Zdroj: | Cellular and Molecular Life Sciences. 76:4995-5009 |
| ISSN: | 1420-9071 1420-682X |
| DOI: | 10.1007/s00018-019-03157-7 |
| Popis: | Protein interacting with Amyloid Precursor Protein (APP) tail 1 (PAT1) also called APPBP2 or Ara 67 has different targets such as APP or androgen receptor and is expressed in several tissues. PAT1 is known to be involved in the subcellular trafficking of its targets. We previously observed in primary neurons that PAT1 is poorly associated with APP at the cell surface. Here we show that PAT1 colocalizes with vesicles close to the cell surface labeled with Rab5, Rab4, EEA1 and Rabaptin-5 but not with Rab11 and Rab7. Moreover, PAT1 expression regulates the number of EEA1 and Rab5 vesicles, and endocytosis/recycling of the transferrin receptor. In addition, low levels of PAT1 decrease the size of transferrin-colocalized EEA1 vesicles with time following transferrin uptake. Finally, overexpression of the APP binding domain to PAT1 is sufficient to compromise endocytosis. Altogether, these data suggest that PAT1 is a new actor in transferrin early endocytosis. Whether this new function of PAT1 may have consequences in pathology remains to be determined. |
| Databáze: | OpenAIRE |
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