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Protein sorting during endocytosis
Abstract
Movement and sorting of proteins along the endocytic pathway is complex. At most branching points in the pathway movement can potentially be multidirectional. For example, a protein passing through the endosomal membrane system has access to transport routes that could take it ‘back’ to the cell surface, ‘forward’ to the lysosomes, or in a ‘lateral’ direction towards the trans Golgi network (TGN). Secondly, movement along the endocytic pathway involves multiple terminal destinations, most notably the cell surface (either apical or basolateral in polarized cells), the lysosomes, or the TGN. Thirdly, in some instances multiple pathways can be used to achieve the same final destination. This is most evident in the case of some lysosomal proteins where targeting to lysosomes can be either intracellular (directly from the TGN) or via the cell surface following internalization.
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The sortilin cytoplasmic domain contains several potential signal sequences conforming to established consensus motifs involved in adaptor protein binding, endocytosis, basolateral targeting and Golgi-endosome sorting.
“Moreover, the sortilin cytoplasmic domain contains several potential signal sequences that conform to established consensus motifs, known to be involved in adaptor protein binding, endocytosis, basolateral targeting and Golgi±endosome sorting (Ktistakis and Roth, 1996).”
From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Ktistakis and Roth, 1996
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Nielsen, M. S., Madsen, P., Christensen, E. I., Nykjær, A., Gliemann, J., Kasper, D., Pohlmann, R., & Petersen, C. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2180 · Cited by 457
Metadata
- Authors
- Ktistakis, N. T., & Roth, M. G.
- Venue
- Protein Targeting
- Publisher
- Oxford University PressOxford
- Published
- 1996-08-22
- Pages
- 176-212
- Cited by
- 1
- References
- 0
- Language
- en
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