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Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins
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“SNX27 also interacts with the SNX-BAR (Bin/Amphiphysin/Rvs) proteins SNX1 and SNX2 [27,28,31,62] and the WASH complex [37] to couple sequence-dependent retrieval of SNX27 cargoes with tubule formation during the process of cargo recycling.”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [28]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Surprisingly, VPS35 suppression resulted in an increase in LRFNs (LRFN1, 2 and 4) at the neuronal surface (Figure 2C) suggesting that SNX27 can act independently to Retromer in the trafficking of a sub-set of cargoes, potentially through the ESCPE-1 complex [27,28].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [28]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“To function, Retromer associates with accessory proteins and cargo adaptors including sorting nexins (SNXs) [24][25][26][27][28][29][30][31][32][33][34], the WASH complex [35][36][37][38][39], RAB GTPase regulators including TBC1D5 and ANKRD27/VARP [40][41][42][43][44][45][46], and RME8 [47].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [28]
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“Rather, structural, biochemical and functional evidence has associated ESCPE-1 in sequence-dependent endosome-to-TGN sorting of the CI-MPR through direct recognition of a bipartite sorting motif localised within the unstructured cytosplasmic tail of this receptor (Kvainickas et al., 2017; Simonetti et al., 2017, 2019).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Simonetti et al., 2019
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“Consistent with the role of SNX5 in the ESCPE-1-mediated endosome-to-TGN transport of the CI-MPR (Kvainickas et al., 2017; Simonetti et al., 2017, 2019), SNX5 knocksideways in SNX5/SNX6 double-knockout HeLa cells led to the time-resolved appearance of a CI-MPR missorting phenotype as defined by a reduced enrichment of the CI-MPR at the Golgin97 or TGN46-labelled TGN with a maximum penetrance at 6”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Simonetti et al., 2019
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“Of these proteins, it is the PX domains of SNX5 and SNX6 that directly bind to the ΦxΩxΦ(x)nΦ sorting motif (where Φ represents hydrophobic amino acids) in CI-MPR to mediate endosome-to-TGN transport (Simonetti et al., 2019).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Simonetti et al., 2019
In the citing paper
“These data therefore support the in vivo evidence that in metazoans retromer and ESCPE-1 have evolved into functionally distinct complexes (Kvainickas et al., 2017; Simonetti et al., 2017, 2019; Strutt et al., 2019).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Simonetti et al., 2019
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Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
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
Self-citationRetriever is a multiprotein complex for retromer-independent endosomal cargo recycling
McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3610 · Cited by 346
Self-citationCCC- and WASH-mediated endosomal sorting of LDLR is required for normal clearance of circulating LDL
Bartuzi, P., Billadeau, D. D., Favier, R., Rong, S., Dekker, D., Fedoseienko, A., Fieten, H., Wijers, M., Levels, J. H., Huijkman, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms10961 · Cited by 205
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
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Cited by
Sorted by citations
The Retromer Complex: From Genesis to Revelations
Seaman, M. N. J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.009 · Cited by 104
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
Self-citationAcute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting
Evans, A. J., Daly, J. L., Anuar, A. N. K., Simonetti, B., & Cullen, P. J. (2020) · Journal of Cell Science · doi:10.1242/jcs.246033 · Cited by 25
Self-citationStructural basis for Retriever-SNX17 assembly and endosomal sorting
Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23
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
Self-citation
Metadata
- Authors
- Simonetti, B., Paul, B., Chaudhari, K., Weeratunga, S., Steinberg, F., Gorla, M., Heesom, K. J., Bashaw, G. J., Collins, B. M., & Cullen, P. J.
- Venue
- Nature Cell Biology
- Published
- 2019-10
- Volume
- 21
- Issue
- 10
- Pages
- 1219-1233
- ISSN
- 1465-7392
- 1476-4679
- PMC
- PMC6778059
- Cited by
- 145
- References
- 5
- Language
- en
- Funders
- Wellcome Trust (083474, 104568/Z/14/2)
- Department of Health | National Health and Medical Research Council (APP1099114)
- Department of Education and Training | Australian Research Council (DP160101743)
- RCUK | Medical Research Council (MR/L007363/1)
- RCUK | MRC | Medical Research Foundation (MR/P018807/1)
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