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Retromer‐mediated recruitment of the WASH complex involves discrete interactions between VPS35 , VPS29, and FAM21
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Abstract
Endosomal trafficking ensures the proper distribution of lipids and proteins to various cellular compartments, facilitating intracellular communication, nutrient transport, waste disposal, and the maintenance of cell structure. Retromer, a peripheral membrane protein complex, plays an important role in this process by recruiting the associated actin‐polymerizing WASH complex to establish distinct sorting domains. The WASH complex is recruited through the interaction of the VPS35 subunit of retromer with the WASH complex subunit FAM21. Here, we report the identification of two separate fragments of FAM21 that interact with VPS35, along with a third fragment that binds to the VPS29 subunit of retromer. The crystal structure of VPS29 bound to a peptide derived from FAM21 shows a distinctive sharp bend that inserts into a conserved hydrophobic pocket with a binding mode similar to that adopted by other VPS29 effectors. Interestingly, despite the network of interactions between FAM21 and retromer occurring near the Parkinson's disease‐linked mutation (D620N) in VPS35, this mutation does not significantly impair the direct association with FAM21 in vitro.
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In all cases, the accessory protein directly associates with Retromer through presentation of PL motifs to the same hydrophobic pocket in VPS29 that accommodates PL motifs from TBC1D5, ANKRD27 and the FAM21 subunit of the WASH complex.
“In all cases, the accessory protein directly associates with Retromer through presentation of PL motifs to the same hydrophobic pocket in VPS29 that accommodates PL motifs from TBC1D5, ANKRD27 and the FAM21 subunit of the WASH complex44,77,82,114.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [114]
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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
Muhammad, A., Flores, I., Zhang, H., Yu, R., Staniszewski, A., Planel, E., Herman, M., Ho, L., Kreber, R., Honig, L. S., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802545105 · Cited by 248
Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome
Healy, M. D., McNally, K. E., Butkovič, R., Chilton, M., Kato, K., Sacharz, J., McConville, C., Moody, E. R. R., Shaw, S., Planelles-Herrero, V. J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.04.003 · Cited by 91
Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis
Muzio, L., Sirtori, R., Gornati, D., Eleuteri, S., Fossaghi, A., Brancaccio, D., Manzoni, L., Ottoboni, L., Feo, L. D., Quattrini, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17524-7 · Cited by 65
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
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Research works printed but not linked: 53
- 10.1016/j.ceb.2019.03.010 · DOI
- 10.1038/s41467-017-01512-5 · DOI
- 10.1126/sciadv.abg4007 · DOI · Paper page
- 10.1073/pnas.1814909116 · DOI
- 10.1038/s41467-020-18773-2 · DOI · Paper page
- 10.1111/tra.12779 · DOI
- 10.1038/s41580-018-0053-7 · DOI · Paper page
- 10.1002/ana.25752 · DOI · Paper page
- 10.1074/jbc.RA120.013672 · DOI
- 10.1107/S0907444910007493 · DOI · Paper page
- 10.1074/jbc.M115.703157 · DOI · Paper page
- 10.1111/tra.12136 · DOI
- 10.1242/jcs.144659 · DOI
- 10.1242/jcs.071472 · DOI · Paper page
- 10.1042/BJ20111761 · DOI · Paper page
- 10.1111/boc.201200038 · DOI
- 10.1038/nsmb.1792 · DOI
- 10.1016/j.devcel.2014.04.010 · DOI · Paper page
- 10.1038/nature06216 · DOI · Paper page
- 10.1091/mbc.e11-12-1059 · DOI · Paper page
- 10.1073/pnas.0913293107 · DOI · Paper page
- 10.1038/ncomms13305 · DOI · Paper page
- 10.1107/S0907444909047337 · DOI · Paper page
- 10.1016/j.str.2020.01.009 · DOI
- 10.1038/s41586-018-0526-z · DOI · Paper page
- 10.1242/jcs.196758 · DOI
- 10.1007/BF02390355 · DOI
- 10.1021/ci200227u · DOI
- 10.1038/ncomms10939 · DOI · Paper page
- 10.1126/sciadv.abf8598 · DOI · Paper page
- 10.1016/j.cell.2016.10.056 · DOI · Paper page
- 10.1107/S0021889807021206 · DOI · Paper page
- 10.1242/jcs.156299 · DOI · Paper page
- 10.1016/j.cub.2014.07.004 · DOI
- 10.1038/nchembio.1508 · DOI · Paper page
- 10.1093/hmg/ddu582 · DOI · Paper page
- 10.1107/S0907444911001314 · DOI
- 10.1016/j.cellsig.2016.10.014 · DOI
- 10.1073/pnas.2118755119 · DOI
- 10.1091/mbc.e14-06-1073 · DOI · Paper page
- 10.1016/j.cell.2010.10.003 · DOI · Paper page
- 10.1073/pnas.1715361115 · DOI
- 10.1242/jcs.217398 · DOI · Paper page
- 10.1006/prep.1998.1003 · DOI
- 10.1016/j.ceb.2018.08.006 · DOI · Paper page
- 10.1002/ana.20667 · DOI · Paper page
- 10.1038/ncb2721 · DOI · Paper page
- 10.1242/jcs.211342 · DOI
- 10.1016/j.ajhg.2011.06.001 · DOI · Paper page
- 10.1073/pnas.1717383115 · DOI
- 10.1016/j.isci.2022.104254 · DOI · Paper page
- 10.1038/ncomms4828 · DOI · Paper page
- 10.1016/j.ajhg.2011.06.008 · DOI · Paper page
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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
- Romano‐Moreno, M., Astorga‐Simón, E. N., Rojas, A. L., & Hierro, A.
- Affiliations
- Center for Cooperative Research in Biosciences (CIC bioGUNE) Bilbao Spain
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2024-04-12
- Volume
- 33
- Issue
- 5
- ISSN
- 0961-8368
- 1469-896X
- PMC
- PMC11010949
- Cited by
- 15
- References
- 5
- Language
- en
- Funders
- Ministerio de Ciencia e Innovación (PID2020‐119132GB‐100)
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