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COMMD1 is linked to the WASH complex and regulates endosomal trafficking of the copper transporter ATP7A
Abstract
COMMD1 deficiency results in defective copper homeostasis, but the mechanism for this has remained elusive. Here we report that COMMD1 is directly linked to early endosomes through its interaction with a protein complex containing CCDC22, CCDC93, and C16orf62. This COMMD/CCDC22/CCDC93 (CCC) complex interacts with the multisubunit WASH complex, an evolutionarily conserved system, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. Interactions between the WASH complex subunit FAM21, and the carboxyl-terminal ends of CCDC22 and CCDC93 are responsible for CCC complex recruitment to endosomes. We show that depletion of CCC complex components leads to lack of copper-dependent movement of the copper transporter ATP7A from endosomes, resulting in intracellular copper accumulation and modest alterations in copper homeostasis in humans with CCDC22 mutations. This work provides a mechanistic explanation for the role of COMMD1 in copper homeostasis and uncovers additional genes involved in the regulation of copper transporter recycling.
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CCC is required for retromer- and retriever-dependent protein trafficking.
“the CCC protein complex, which consists of CCDC22, CCDC93, and any of the 10 COMMD proteins, is required for retromer- and retriever-dependent protein trafficking27–32”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [27]
The Results section (‘The CCC complex regulates ATP7A trafficking’; page unavailable) shows that loss of CCC components disrupts trafficking of retromer cargo, including ATP7A and TGN46. The paper also identifies CCDC22, CCDC93, and COMMD proteins as CCC-associated components. Our copy does not address retriever-dependent trafficking, so that part of the claim is unsupported by this source. (LLM, conf=0.89)
Experimental — accuracy not yet measuredCCC recruitment to endosomal membranes is dependent on the WASH complex.
“CCC recruitment to endosomal membranes is dependent on the pentameric Wiskott-Aldrich syndrome protein and SCAR homologue (WASH) complex27”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [27]
The Results section, “FAM21 is required for endosomal recruitment of the CCC complex” (page unavailable), concludes that the WASH-complex subunit FAM21 is required for CCC recruitment to endosomes. But it also reports that loss of Wash did not abolish COMMD1 endosomal localization, so dependence on the WASH complex as a whole is broader than the demonstrated finding. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe CCC protein complex consists of CCDC22, CCDC93, and any of the 10 COMMD proteins.
“the CCC protein complex, which consists of CCDC22, CCDC93, and any of the 10 COMMD proteins”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [27]
The Results ('Identification of the CCC complex') report that all 10 COMMD proteins interact with CCDC93, and the Discussion identifies COMMD proteins, CCDC22, and CCDC93 as core components. But the Discussion also includes C16orf62 in the core composition, so the claim's apparently complete list omits a component. Page numbers are not provided in our copy's passages. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCCDC22, CCDC93, and seven COMMDs form the CCC complex, which is required for endosomal recycling of certain cargos including copper transporters, Notch family members and LDLR.
“These form the CCC complex39, shown to be required for the endosomal recycling of certain cargos, including copper transporters39, Notch family members39, 40 and LDLR41.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [39]
The Results (Identification of the CCC complex; The CCC complex regulates ATP7A trafficking) identify CCDC22, CCDC93 and COMMD proteins as CCC components and show that the complex regulates endosomal trafficking of the copper transporter ATP7A. The paper does not establish a composition of exactly seven COMMD proteins or address Notch recycling. LDLR is cited separately to reference 41 in the printed sentence, so that portion is not attributed to this source. (LLM, conf=0.87)
Experimental — accuracy not yet measuredThe first conserved patch is on the CCDC22-CCDC93 coiled-coil structure, lying adjacent to DENND10, aligning closely with a region required for interacting with FAM21 of the WASH complex.
“The first is a patch on the CCDC22-CCDC93 coiled-coil structure, lying adjacent to DENND10 (Figure S7B) aligning closely with a region required for interacting with FAM21 of the WASH complex.65”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [65]
The Results section, “The carboxy-terminal ends of CCDC22/CCDC93 are responsible for FAM21 binding” (page unavailable), maps regions of both proteins that interact with FAM21. It does not identify a conserved patch on their coiled-coil structure, place that patch adjacent to DENND10, or establish that it aligns with the FAM21-interacting region. (LLM, conf=0.87)
Experimental — accuracy not yet measured
The structure is consistent with truncation analyses that found N-terminal regions of CCDC22 and CCDC93 could interact with COMMD proteins but not Retriever.
“The structure is also consistent with truncation analyses that found N-terminal regions of CCDC22 and CCDC93 could interact with COMMD proteins but not Retriever.21,65”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [65]
In Results, ‘Organization of the CCC complex’ (page unavailable), the truncation analysis places CCDC22–COMMD1 binding in CCDC22’s N-terminal region and describes N-terminal interactions between CCDC22 and CCDC93. The copy also reports that CCDC93 interacts with COMMD proteins, but it does not establish here that CCDC93’s N-terminal region mediates that interaction. It does not address whether either N-terminal region binds Retriever. (LLM, conf=0.86)
Experimental — accuracy not yet measuredEvidence that CCDC22(T17A), CCDC22(Y557C), and VPS35L(A830T) perturb endosomal recycling of LRP1 and LDLR and lead to hypercholesterolemia.
“Taken alongside evidence that CCDC22(T17A), CCDC22(Y557C), and VPS35L(A830T) perturb endosomal recycling of LRP1 and LDLR and lead to hypercholesterolemia,11,65”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [65]
The Results section (no page number available in our copy) shows that CCDC22(T17A) fibroblasts have altered ATP7A trafficking and loss of endosomal COMMD1 localization. It does not establish that CCDC22(T17A), CCDC22(Y557C), or VPS35L(A830T) disrupt recycling of LRP1 or LDLR or lead to hypercholesterolemia; the trafficking results here concern ATP7A and TGN46. (LLM, conf=0.86)
Experimental — accuracy not yet measuredRetriever, together with the dodecameric CCDC22, CCDC93, COMMD (CCC) complex and DENND10, forms the 16-subunit Commander super-assembly.
“that together with the dodecameric CCDC22, CCDC93, COMMD (CCC) complex and DENND10, forms the 16-subunit Commander super-assembly7–12”
From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [7]
The Results section, “Identification of the CCC complex” (page unavailable), supports a CCC complex involving CCDC22, CCDC93 and COMMD proteins, including interactions with all 10 human COMMD family members. The copy does not establish that this is a dodecameric complex or that it joins Retriever and DENND10 in a 16-subunit Commander super-assembly; it instead names C16orf62 among the CCC components. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe common labelling of the WASH complex by both Retromer and Retriever is consistent with their known biochemical association and physical co-localisation to the retrieval sub-domain and the central role of actin polymerisation and actin turnover in Retromer- and Retriever-dependent cargo sorting.
“Building on this, the common labelling of the WASH complex by both Retromer and Retriever (Fig. 2E) is entirely consistent with their known biochemical association and physical co-localisation to the retrieval sub-domain and the central role of actin polymerisation and actin turnover in Retromer- and Retriever-dependent cargo sorting17,19,24,56–58.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [17]
The Introduction says retromer recruits WASH to endosomes and that WASH promotes branched F-actin deposition for receptor trafficking. The Results section on early-endosome localisation places WASH and retromer in the same subcompartment. Our copy does not address Retriever or actin turnover in Retriever-dependent sorting, so it supports only the retromer-related portion of the attributed claim. (LLM, conf=0.87)
Experimental — accuracy not yet measuredEndosomal cargo retrieval and recycling are orchestrated by several multi-protein assemblies including SNX27-Retromer and SNX3-Retromer, SNX17-Retriever and associated Commander super-assembly, the WASH complex and its regulatory MUST complex, and the SNX-BAR proteins and ESCPE-1.
“Orchestrating endosomal cargo retrieval and recycling are several multi-protein assemblies that include sorting nexin-27 (SNX27)-Retromer and SNX3-Retromer8–16, SNX17-Retriever and associated Commander super-assembly17–22, the branched F-actin polymerising WASH complex and its regulatory MAGE-L2/USP7/TRIM27 (MUST) complex23–25, and the SNX-BAR proteins and endosomal sorting complex required for ex”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [17]
The Introduction (page unavailable) describes SNX27–Retromer and the WASH complex as participants in endosomal cargo trafficking. The Results (page unavailable) show that the CCC complex interacts with WASH and regulates trafficking of ATP7A and TGN46. Our copy does not identify CCC as part of an SNX17–Retriever–Commander super-assembly or describe a MUST complex, so it supports only part of the broader list. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe NN-CH domain of CCDC22 consistently occupies the space between the V-shaped CC3 and CC4, irrespective of the presence of VPS35L.
“In addition to the VBD, the small globular domain located at the N-terminus of CCDC22, known as the NDC80-NUF2 calponin homology (NN-CH) domain16, consistently occupies the space between the V-shaped CC3 and CC4, irrespective of the presence of VPS35L (Fig. 5A–B).”
From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [16]
The CCC complex has been recognized for its role in regulating endosomal recycling of various cargos.
“The CCC complex is a molecular assembly that has been recognized for its role in regulating endosomal recycling of various cargos20,27,30–32,34”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [27]
Additional proteins identified included CCC complex associated C16orf62, DSCR3 and retromer subunit VPS29.
“Additional proteins identified from our proteomics included the CCC complex associated C16orf6239, DSCR3 and the retromer subunit VPS29.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [39]
WASH recruits CCC complex through direct interactions of CCDC93 with WASH complex component FAM21.
“WASH recruits the CCC complex through direct interactions of CCDC93 with the WASH complex component FAM2139.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [39]
Retriever interacts with FAM21 through its interactions with CCC complex.
“Our data is consistent with retriever interacting with FAM21 through its interactions with the CCC complex39.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [39]
VPS26C plays a central role in the endosomal association and function of Commander through a mechanism that may include association with the cargo adaptor SNX17, the WASH complex, and/or an inherent ability of VPS26C to associate with membranes.
“VPS26C therefore plays a central role in the endosomal association and function of Commander through a mechanism that may include association with the cargo adaptor SNX17,6 the WASH complex,65 and/or an inherent ability of VPS26C to associate with membranes.60”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [65]
The CCC complex is physically associated with the WASH complex through binding of CCDC93 and CCDC22 to WASHC2.
“the CCC complex is physically associated with the WASH complex through the binding of the CCC components CCDC93 and CCDC22 to the WASH subunit WASHC2 (FAM21) (5).”
From The hepatic WASH complex is required for efficient plasma LDL and HDL cholesterol clearance (2019) · cites this paper as [5]
Retriever is a stable heterotrimer of VPS26C, VPS35L and VPS29.
“Retriever is an essential cargo sorting complex and is a stable heterotrimer of VPS26C, VPS35L and VPS29”
From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [7]
The Introduction describes retromer as a VPS26–VPS29–VPS35 cargo-selection trimer, not Retriever. Searches for Retriever, VPS26C, and VPS35L found no passage in our copy addressing Retriever’s composition or stability. (LLM, conf=0.76)
Experimental — accuracy not yet measuredThe CCC complex is a 12-protein assembly composed of CCDC22, CCDC93, and ten COMMD proteins.
“The WASH complex is regulated by the COMMD-CCDC22-CCDC93 or CCC complex [8], a 12-protein assembly that limits the endosomal localization and actin polymerization activity of the WASH complex [14].”
From CCDC22 mutations that impair COMMD binding cause attenuated 3C/Ritscher-Schinzel syndrome (2025) · cites this paper as [8]
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Metadata
- Authors
- Phillips-Krawczak, C. A., Singla, A., Starokadomskyy, P., Deng, Z., Osborne, D. G., Li, H., Dick, C. J., Gomez, T. S., Koenecke, M., Zhang, J.-S., Dai, H., Sifuentes-Dominguez, L. F., Geng, L. N., Kaufmann, S. H., Hein, M. Y., Wallis, M., McGaughran, J., Gecz, J., Sluis, B. V. D., Billadeau, D. D., & Burstein, E.
- Venue
- Molecular Biology of the Cell
- Published
- 2015-01
- Volume
- 26
- Issue
- 1
- Pages
- 91-103
- ISSN
- 1059-1524
- 1939-4586
- PMC
- PMC4279232
- Cited by
- 246
- References
- 3
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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