The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
SNX-1 and RME-8 oppose the assembly of HGRS-1/ESCRT-0 degradative microdomains on endosomes
Abstract
Significance: Endosomes are membrane-bound organelles that are important for nutrient uptake, protein and lipid sorting, and signal transduction. When integral membrane proteins have reached the endosomal system, they can be sent to the lysosome for degradation or recycled for reuse. Here we provide insight into how the machinery important for reuse controls the machinery that mediates degradation. We show that these opposing functions occupy physically distinct regions of the endosomes, termed microdomains, and that this separation is likely to provide a physical framework for a variety of sorting decisions.
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Specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches.
“A number of studies have shown that specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches9,34–44”
From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [42]
The Results report distinct ESCRT-associated degradative and retromer-associated recycling microdomains on the same endosomes. The Discussion mentions WASH accumulating on endosomal tubules, but does not establish WASH-dependent actin patches as a separate recycling domain; our copy does not support the claim's inclusion of Retriever or the CCC complex. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCore retrieval and recycling complexes localise to specific retrieval sub-domains that are physically distinct from ESCRT-demarcated degradative sub-domains on the same endosome.
“On the limiting membrane of endosomes, electron and light microscopy has established that core retrieval and recycling complexes localise to specific retrieval sub-domains that, while present on the same endosome, are physically distinct from ESCRT-demarcated degradative sub-domains19,32–37.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [37]
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Retromer: A Master Conductor of Endosome Sorting
Burd, C., & Cullen, P. J. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016774 · Cited by 435
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Cited by
Sorted by citations
To degrade or not to degrade: Mechanisms and significance of endocytic recycling
Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590
Endosomal retrieval of cargo: Retromer is not alone
McNally, K. E., & Cullen, P. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.005 · Cited by 169
Receptor Recycling by Retromer
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2023) · Molecular and Cellular Biology · doi:10.1080/10985549.2023.2222053 · Cited by 36
Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway
Butkovič, R., Walker, A. P., Healy, M. D., McNally, K. E., Liu, M., Veenendaal, T., Kato, K., Liv, N., Klumperman, J., Collins, B. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50971-0 · Cited by 26
Retromer dysfunction at the nexus of tauopathies
Carosi, J. M., Denton, D., Kumar, S., & Sargeant, T. J. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-020-00727-2 · Cited by 16
Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation
Antón-Plágaro, C., Chen, K.-E., Guo, Q., Liu, M., Evans, A. J., Lewis, P. A., Heesom, K. J., Wilkinson, K. A., Collins, B. M., & Cullen, P. J. (2025) · Nature Communications · doi:10.1038/s41467-025-61802-1 · Cited by 14
Metadata
- Authors
- Norris, A., Tammineni, P., Wang, S., Gerdes, J., Murr, A., Kwan, K. Y., Cai, Q., & Grant, B. D.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-01-04
- Volume
- 114
- Issue
- 3
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 90
- References
- 2
- Language
- en
- Funders
- HHS | NIH | National Institute of General Medical Sciences (GM067237, GM103995, 5F32GM096599)
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