Subcellular Trafficking of Mammalian Lysosomal Proteins: An Extended View
| Autor: | Catherine Staudt, Emeline Puissant, Marielle Boonen |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Hydrolases Endosome Review Protein Sorting Signals Biology Alternative receptor mannose 6-phosphate Catalysis lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences Mannose 6-phosphate trafficking Cell surface receptor Organelle Animals Humans unconventional Physical and Theoretical Chemistry Tyrosine Receptor lcsh:QH301-705.5 Molecular Biology Spectroscopy Mammals Trafficking Mannose 6-phosphate receptor Organic Chemistry Membrane Proteins Sorting motif alternative receptor sorting motif General Medicine Lysosome Transmembrane protein Computer Science Applications Cell biology Protein Transport 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 Biochemistry Unconventional lysosome Lysosomes Protein Processing Post-Translational Biogenesis |
| Zdroj: | International Journal of Molecular Sciences, Vol 18, Iss 1, p 47 (2016) International Journal of Molecular Sciences Staudt, C, Puissant, E & Boonen, M 2017, ' Subcellular trafficking of mammalian lysosomal proteins : An extended view ', International Journal of Molecular Sciences, vol. 18, no. 1, 47 . https://doi.org/10.3390/ijms18010047 |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms18010047 |
| Popis: | Lysosomes clear macromolecules, maintain nutrient and cholesterol homeostasis, participate in tissue repair, and in many other cellular functions. To assume these tasks, lysosomes rely on their large arsenal of acid hydrolases, transmembrane proteins and membrane-associated proteins. It is therefore imperative that, post-synthesis, these proteins are specifically recognized as lysosomal components and are correctly sorted to this organelle through the endosomes. Lysosomal transmembrane proteins contain consensus motifs in their cytosolic regions (tyrosine-or dileucine-based) that serve as sorting signals to the endosomes, whereas most lysosomal acid hydrolases acquire mannose 6-phosphate (Man-6-P) moieties that mediate binding to two membrane receptors with endosomal sorting motifs in their cytosolic tails. These tyrosine-and dileucine-based motifs are tickets for boarding in clathrin-coated carriers that transport their cargo from the trans-Golgi network and plasma membrane to the endosomes. However, increasing evidence points to additional mechanisms participating in the biogenesis of lysosomes. In some cell types, for example, there are alternatives to the Man-6-P receptors for the transport of some acid hydrolases. In addition, several “non-consensus” sorting motifs have been identified, and atypical transport routes to endolysosomes have been brought to light. These “unconventional” or “less known” transport mechanisms are the focus of this review. |
| Databáze: | OpenAIRE |
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