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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]
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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]
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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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Research works printed but not linked: 64
- Goldenring, J. R. Recycling endosomes. Curr. Opin. Cell Biol. 35, 117–122 (2015). · DOI
- Cullen, P. J. & Steinberg, F. To degrade or not to degrade: mechanisms and significance of endocytic recycling. Nat. Rev. Mol. Cell Biol. 19, 679–696 (2018). · DOI · Paper page
- Behnia, R. & Munro, S. Organelle identity and the signposts for membrane traffic. Nature 438, 597–604 (2005). · DOI
- Phillips-Krawczak, C. A. et al. COMMD1 is linked to the WASH complex and regulates endosomal trafficking of the copper transporter ATP7A. Mol. Biol. Cell 26, 91–103 (2015). · DOI · Paper page
- Meyer, C. et al. μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193–2203 (2000). · DOI · Paper page
- Seaman, M. N. J., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665–681 (1998). · DOI · Paper page
- Seaman, M. N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111–122 (2004). · DOI · Paper page
- Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R. & Bonifacino, J. S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123–133 (2004). · DOI · Paper page
- Strochlic, T. I., Setty, T. G., Sitaram, A. & Burd, C. G. Grd19/Sns3p functions as a cargo-specific adapter for retromer-dependent endocytic recycling. J. Cell Biol. 177, 115–125 (2007). · DOI · Paper page
- Harterink, M. et al. A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nat. Cell Biol. 13, 914–923 (2011). · DOI · Paper page
- Temkin, P. et al. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat. Cell Biol. 13, 715–721 (2011). · DOI · Paper page
- Steinberg, F. et al. A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nat. Cell Biol. 15, 461–471 (2013). · DOI · Paper page
- Lucas, M. et al. Structural mechanism for cargo recognition by the retromer complex. Cell 167, 1623–1635 (2016). · DOI · Paper page
- Purushothaman, L. K. & Ungermann, C. Cargo induces retromer-mediated membrane remodelling on membranes. Mol. Biol. Cell 29, 2709–2719 (2018). · DOI · Paper page
- Kovtun, O. et al. Structure of the membrane-assembled retromer coat determined by cryo-electron tomography. Nature 561, 561–564 (2018). · DOI · Paper page
- Carlton, J. et al. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr. Biol. 14, 1791–1800 (2004). · DOI · Paper page
- Wassmer, T. et al. A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45–54 (2007). · DOI · Paper page
- Wassmer, T. et al. The retromer coat complex coordinates endosomal sorting and dynein-mediated transport with carrier recognition by the trans-Golgi network. Dev. Cell 17, 110–122 (2009). · DOI
- van Weering, J. R. et al. Molecular basis for SNX–BAR-mediated assembly of distinct endosomal sorting tubules. EMBO J. 31, 4466–4480 (2012). · DOI · Paper page
- Simonetti, B., Danson, C. M., Heesom, K. J. & Cullen, P. J. Sequence-dependent cargo recognition by SNX–BARs mediates retromer-independent transport of CI-MPR. J. Cell Biol. 216, 3695–3712 (2017). · DOI · Paper page
- Kvainickas, A. et al. Cargo-selective SNX–BAR proteins mediate retromer trimer independent retrograde transport. J. Cell Biol. 216, 3677–3693 (2017). · DOI · Paper page
- Teasdale, R. D., Loci, D., Houghton, F., Karlsson, L. & Gleeson, P. A. A large family of endosome-localised proteins related to sorting nexin 1. Biochem. J. 358, 7–16 (2001). · DOI
- Elwell, C. A. et al. Chlamydia interfere with an interaction between the mannose-6-phosphate receptor and sorting nexins to counteract host restriction. eLife 6, e22709 (2017). · DOI
- Paul, B. et al. Structural basis for the hijacking of endosomal sorting nexin proteins by Chlamydia trachomatis. eLife 6, e22311 (2017). · DOI
- Sun, Q. et al. Structural and functional insights into sorting nexin 5/6 interaction with bacterial effector IncE. Signal Transduct. Target. Ther. 2, 17030 (2017). · DOI
- Seaman, M. N. Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval. J. Cell Sci. 120, 2378–2389 (2007). · DOI
- Coutinho, M. F., Prata, M. J. & Alves, S. Mannose-6-phosphate pathway: a review on its role in lysosomal function and dysfunction. Mol. Genet. Metab. 105, 542–550 (2012). · DOI
- Itai, N. et al. The phosphorylation of sorting nexin 5 at serine 226 regulates retrograde transport and macropinocytosis. PLoS One 13, e0207205 (2018). · DOI
- Chandra, M. et al. Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities. Nat. Commun. 10, 1528 (2019). · DOI
- Blockus, H. & Chedotal, A. Slit-Robo signaling. Development 143, 3037–3044 (2016). · DOI
- Deng, H. X. et al. Identification of TMEM230 mutations in familial Parkinson’s disease. Nat. Genet. 48, 733–739 (2016). · DOI
- Wojciech, S. et al. The orphan GPR50 receptor promotes constitutive TGFβ receptor signaling and protects against cancer development. Nat. Commun. 9, 1216 (2018). · DOI
- Fan, X., Labrador, J. P., Hing, H. & Bashaw, G. J. Slit stimulation recruits Dock and Pak to the roundabout receptor and increases rac activity to regulate axon repulsion at the CNS midline. Neuron 40, 113–127 (2003). · DOI
- Kidd, T., Bland, K. S. & Goodman, C. S. Slit is the midline repellent for the Robo receptor in Drosophila. Cell 96, 785–794 (1999). · DOI
- Coleman, H. A., Labrador, J. P., Chance, R. K. & Bashaw, G. J. The Adam family metalloprotease Kuzbanian regulates the cleavage of the roundabout receptor to control axon repulsion at the midline. Development 137, 2417–2426 (2010). · DOI
- Hernandez-Fleming, M., Rohrbach, E. & Bashaw, G. J. Sema-1a reverse signaling promotes midline crossing in response to secreted Semaphorins. Cell Rep. 18, 174–184 (2017). · DOI
- Klumperman, J. & Raposo, G. The complex ultrastrutcure of the endolysosomal system. Cold Spring Harb. Perspect. Biol. 6, a016857 (2014). · DOI
- Bright, N. A., Davis, L. J. & Luzio, J. P. Endolysosomes are the principal intracellular sites of acid hydrolase activity. Curr. Biol. 26, 2233–2245 (2016). · DOI
- Mari, M. et al. SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-phosphate receptors. Traffic 9, 380–393 (2008). · DOI · Paper page
- Johannes, L. & Wunder, C. Retrograde transport: two (or more) roads diverged in an endosomal tree? Traffic 12, 956–962 (2011). · DOI
- Seaman, M. N. J. Retromer and the cation-independent mannose 6-phosphate receptor—time for a trial separation? Traffic 19, 150–152 (2018). · DOI
- Carroll, K. S. et al. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 292, 1373–1376 (2001). · DOI
- Wan, L. et al. PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localisation. Cell 94, 205–216 (1998). · DOI
- Robinson, M. S., Sahlender, D. A. & Foster, S. D. Rapid inactivation of proteins by rapamycin-induced rerouting to mitochondria. Dev. Cell 18, 324–331 (2010). · DOI
- Hirst, J. et al. Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15. Mol. Biol. Cell 24, 2558–2569 (2013). · DOI
- Gallon, M.et al. A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer. Proc. Natl Acad. Sci. USA 111, E3604–13 (2014). · DOI · Paper page
- Gomez, T. S. & Billadeau, D. D. A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev. Cell 17, 699–711 (2009). · DOI · Paper page
- Harbour, M. E., Breusegem, S. Y. & Seaman, M. N. Recruitment of the endosomal WASH complex is mediated by the extended ‘tail’ of Fam21 binding to the retromer protein Vps35. Biochem. J. 442, 209–220 (2012). · DOI · Paper page
- Jia, D., Gomez, T. S., Billadeau, D. D. & Rosen, M. K. Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer. Mol. Biol. Cell 23, 2352–2361 (2012). · DOI · Paper page
- McGough, I. J. et al. Identification of molecular heterogeneity in SNX27-retromer-mediated endosome-to-plasma membrane recycling. J. Cell Sci. 127, 4940–4953 (2014). · DOI · Paper page
- Kvainickas, A. et al. Retromer- and WASH-dependent sorting of nutrient transporters requires a multivalent interaction network with ANKRD50. J. Cell Sci. 130, 382–395 (2017). · DOI
- Cui, Y. et al. Retromer has a selective function in cargo sorting via endosome transport carriers. J. Cell Biol. 218, 615–631 (2019). · DOI · Paper page
- Hirst, J. et al. Distinct and overlapping roles for AP-1 and GGAs revealed by the ‘knocksideways’ system. Curr. Biol. 22, 1711–1716 (2012). · DOI · Paper page
- Hirst, J., Itzhak, D. N., Antrobus, R., Borner, G. H. H. & Robinson, M. S. Role of the AP-5 adaptor protein complex in late endosome-to-Golgi retrieval. PLoS Biol. 16, e2004411 (2018). · DOI
- Varandas, K. C., Irannejad, R. & von Zastrow, M. Retromer endosome exit domains serve multiple trafficking destinations and regulate local G protein activation by GPCRs. Curr. Biol. 26, 3129–3142 (2016). · DOI · Paper page
- Shafaq-Zadah, M. et al. Presistent cell migration and adhesion rely on retrograde transport of β1-integrin. Nat. Cell Biol. 18, 54–64 (2016). · DOI
- Mirrashidi, K. M. et al. Global mapping of the Inc-human interactome reveals that retromer restricts Chlamydia infection. Cell Host Microbe 18, 109–121 (2015). · DOI
- Subbarayal, P. et al. EphrinA2 receptor (EphA2) is an invasion and intracellular signalling receptor for Chlamydia trachomatis. PLoS Pathog. 11, e1004846 (2015). · DOI
- Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731–740 (2016). · DOI · Paper page
- Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R. & Leslie, A. G. iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 67, 271–281 (2011). · DOI
- Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D Biol. Crystallogr. 69, 1204–1214 (2013). · DOI
- McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007). · DOI · Paper page
- Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126–2132 (2004). · DOI · Paper page
- Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94–106 (2011). · DOI
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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-citationJones, E., Adams, H., Chen, K.-E., Maroof, F., Ibbotson, T. M., Nakamura, Y., Banks, P. J., Healy, M. D., Lewis, P. A., Heesom, K. J., et al. (2026) · doi:10.64898/2026.05.14.724903
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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