Retromer has a selective function in cargo sorting via endosome transport carriers
| العنوان: | Retromer has a selective function in cargo sorting via endosome transport carriers |
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| المؤلفون: | Markus C. Kerr, Robert G. Parton, Julian M. Carosi, Rohan D. Teasdale, Nicholas Ariotti, Timothy J. Sargeant, Zhe Yang, Yi Cui |
| المساهمون: | Cui, Yi, Carosi, Julian M, Yang, Zhe, Ariotti, Nicholas, Kerr, Markus C, Parton, Robert G, Sargeant, Timothy J, Teasdale, Rohan D |
| المصدر: | The Journal of Cell Biology |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | SNX27, Retromer, Endosome, Protein subunit, Biological Transport, Active, Endosomes, Biology, Autoantigens, Receptor, IGF Type 2, Article, 03 medical and health sciences, VPS35, 0302 clinical medicine, lysosomal, Lysosome, medicine, Humans, Sorting Nexins, Research Articles, 030304 developmental biology, 0303 health sciences, transport carriers, Peripheral membrane protein, Autophagy, Golgi Matrix Proteins, Cell Biology, Cell biology, medicine.anatomical_structure, cargo sorting, Multiprotein Complexes, Lysosomes, 030217 neurology & neurosurgery, HeLa Cells |
| الوصف: | The molecular actions of retromer in the endolysosomal system remain unclear and controversial. Cui et al. demonstrate the essential role of retromer in the selective incorporation of cargo into a specific type of endosome transport carrier and the maintenance of lysosomal function. Retromer is a peripheral membrane protein complex that coordinates multiple vesicular trafficking events within the endolysosomal system. Here, we demonstrate that retromer is required for the maintenance of normal lysosomal morphology and function. The knockout of retromer subunit Vps35 causes an ultrastructural alteration in lysosomal structure and aberrant lysosome function, leading to impaired autophagy. At the whole-cell level, knockout of retromer Vps35 subunit reduces lysosomal proteolytic capacity as a consequence of the improper processing of lysosomal hydrolases, which is dependent on the trafficking of the cation-independent mannose 6-phosphate receptor (CI-M6PR). Incorporation of CI-M6PR into endosome transport carriers via a retromer-dependent process is restricted to those tethered by GCC88 but not golgin-97 or golgin-245. Finally, we show that this retromer-dependent retrograde cargo trafficking pathway requires SNX3, but not other retromer-associated cargo binding proteins, such as SNX27 or SNX-BAR proteins. Therefore, retromer does contribute to the retrograde trafficking of CI-M6PR required for maturation of lysosomal hydrolases and lysosomal function. |
| تدمد: | 1540-8140 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e5bf383862e6db47c08665c0f55e1a https://pubmed.ncbi.nlm.nih.gov/30559172 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....64e5bf383862e6db47c08665c0f55e1a |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15408140 |
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