Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
Open accessAbstract
Following endocytosis into the endosomal network, integral membrane proteins undergo sorting for lysosomal degradation or are retrieved and recycled back to the cell surface. Here we describe the discovery of an ancient and conserved multiprotein complex that orchestrates cargo retrieval and recycling and, importantly, is biochemically and functionally distinct from the established retromer pathway. We have called this complex 'retriever'; it is a heterotrimer composed of DSCR3, C16orf62 and VPS29, and bears striking similarity to retromer. We establish that retriever associates with the cargo adaptor sorting nexin 17 (SNX17) and couples to CCC (CCDC93, CCDC22, COMMD) and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of α 5 β 1 integrin. Through quantitative proteomic analysis, we identify over 120 cell surface proteins, including numerous integrins, signalling receptors and solute transporters, that require SNX17-retriever to maintain their surface levels. Our identification of retriever establishes a major endosomal retrieval and recycling pathway.
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CG9951's human homolog CDCC22 has been recently found to be a subunit of the retriever complex that acts in endosomal transport, and missense mutations in CDCC22 cause intellectual disability.
“These include CG9951, whose human homolog CDCC22 has been recently found to be a subunit of the retriever complex that acts in endosomal transport. Missense mutations in CDCC22 causing intellectual disability [81,82].”
From Functional unknomics: Systematic screening of conserved genes of unknown function (2023) · cites this paper as [81]
The Results sections on proteomic identification and retriever assembly identify CCDC22 as a component of the CCC complex, while retriever consists of DSCR3, C16orf62 and VPS29. The paper links CCC to endosomal recycling, but explicitly distinguishes it from retriever; the passages found do not address whether CCDC22 missense mutations cause intellectual disability. (LLM, conf=0.87)
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- Authors
- McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., Morris, L. L., Singla, A., Overlee, B. L., Heesom, K. J., Sessions, R., Banks, L., Collins, B. M., Berger, I., Billadeau, D. D., Burstein, E., & Cullen, P. J.
- Affiliations
- University of Bristol (GB)
- The University of Texas Southwestern Medical Center (US)
- University of Freiburg (DE)
- The University of Queensland (AU)
- International Centre for Genetic Engineering and Biotechnology (IT)
- Mayo Clinic (US)
- Corresponding author
- Steinberg, Florian
- Burstein, Ezra
- Cullen, Peter J.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2017-09-11
- Volume
- 19
- Issue
- 10
- Pages
- 1214-1225
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC5790113
- OpenAlex
- W2754145575
- Cited by
- 346
- References
- 62
- Citations by year
- 2026: 18 · 2025: 49 · 2024: 49 · 2023: 35 · 2022: 43 · 2021: 36 · 2020: 45 · 2019: 36 · 2018: 30 · 2017: 5
- FWCI
- 16.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Bristol Research (University of Bristol) (acceptedVersion, other-oa)
- Explore Bristol Research (acceptedVersion, other-oa)
- Funders
- Wellcome Trust (104568, 089928, 104568/Z/14/Z)
- Medical Research Council (MR/K018299/1, MR/P018807/1)
- National Institute of Allergy and Infectious Diseases (R01AI065474)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073639, K01DK106346, R01DK107733, T32DK007745)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- SNX17, VPS29, WASH complex, integrin recycling, alpha5beta1 integrin, endosomal sorting
- MeSH terms
- Animals, Cell Membrane, Drosophila melanogaster, HeLa Cells, Humans, Kinetics, Models, Molecular, Neoplasm Proteins, Protein Binding, Proteins, Endosomes, Structure-Activity Relationship, Transfection, Protein Transport, Drosophila Proteins, Animals, Genetically Modified, Vesicular Transport Proteins, RNA Interference, Proteomics, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Protein Interaction Domains and Motifs, Protein Stability, HEK293 Cells, Sorting Nexins, Proteolysis
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