COMMD5/HCaRG Hooks Endosomes on Cytoskeleton and Coordinates EGFR Trafficking

Campion, Carole G.; Zaoui, Kossay; Verissimo, Thomas; Cossette, Suzanne; Matsuda, Hiroyuki; Solban, Nicolas; Hamet, Pavel; Tremblay, Johanne

doi:10.1016/j.celrep.2018.06.056

Cited by 22 publications

(39 citation statements)

References 47 publications

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“…This result is in agreement with the previously published proteomics data showing that WASH levels are increased in hepatocytes from Commd1 and Commd6 tissue-specific knockout mice that show defective LDLR recycling 32 . Furthermore, they are in agreement with a recent study that identified a number of alterations in cytoskeletal structure in COMMD5-deficient cells 61 . Altogether these data suggest that the enhanced endosomal accumulation of WASH in CCC-deficient states is physiologically detrimental.…”

Section: Discussionsupporting

confidence: 93%

Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling

et al. 2019

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Protein recycling through the endolysosomal system relies on molecular assemblies that interact with cargo proteins, membranes, and effector molecules. Among them, the COMMD/CCDC22/CCDC93 (CCC) complex plays a critical role in recycling events. While CCC is closely associated with retriever, a cargo recognition complex, its mechanism of action remains unexplained. Herein we show that CCC and retriever are closely linked through sharing a common subunit (VPS35L), yet the integrity of CCC, but not retriever, is required to maintain normal endosomal levels of phosphatidylinositol-3-phosphate (PI(3)P). CCC complex depletion leads to elevated PI(3)P levels, enhanced recruitment and activation of WASH (an actin nucleation promoting factor), excess endosomal F-actin and trapping of internalized receptors. Mechanistically, we find that CCC regulates the phosphorylation and endosomal recruitment of the PI(3)P phosphatase MTMR2. Taken together, we show that the regulation of PI(3)P levels by the CCC complex is critical to protein recycling in the endosomal compartment.

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Section: Discussionsupporting

confidence: 93%

Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling

et al. 2019

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“…Taken together this data supports the notion that an important role of Commander is to facilitate trafficking between endosomes and the Golgi. Further evidence for a role in endosomal trafficking is the interaction of Commd5 with the small GTPase Rab5 . Commd5 depletion disrupts both the F‐actin and microtubule cytoskeletons and results in Rab5‐positive endosomes more peripherally localised in the cell.…”

Section: Retriever CCC and The Commander Complexmentioning

confidence: 99%

“…Among the various COMMD proteins the sequence of this HN domain is highly variable, indeed only through secondary structure predictions was it possible to show the domain is structurally similar in all family members. To date the only potential ligands for the HN domain that have been identified are Rab5 and tubulin binding to Commd5 and Commd1 . Its high degree of sequence variability suggests it may impart either specific functions to the different homologues, or that it may help define the precise architecture and stoichiometry of larger COMMD oligomers.…”

Section: Structures Of the Commd Proteinsmentioning

confidence: 99%

Towards a molecular understanding of endosomal trafficking by Retromer and Retriever

Chen

Healy

Collins

2019

Traffic

152

144

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www.traf c.dkCover legend: Retromer is essen al in all eukaryotes for the traffi cking of transmembrane proteins within membrane tubules. Cryoelectron microscopy was used to show how retromer assembles with membrane-bound sor ng nexin proteins to form these membrane tubules. The picture shows a modelled segment of the retromersor ng nexin coat. See Chen et al. (Traffi c 2019; 20(7):465-478). Read the full ar cle on Aim and ScopeTraffic encourages and facilitates the publication of papers covering the cell biology of intracellular transport in health and disease. Areas of interest include protein, nucleic acid and lipid traffic, molecular motors, intracellular pathogens, intracellular proteolysis, nuclear import and export, cytokinesis and the cell cycle, protein translocation, antigen processing and presentation, organelle biogenesis, metabolism, cell polarity and organization, and organelle movement.All aspects of the structural, molecular biology, biochemistry, genetics, morphology, intracellular signaling and relationship to hereditary or infectious diseases will be covered. Manuscripts must provide a clear conceptual or mechanistic advance. The editors will reject papers that require major changes, including addition of significant experimental data or other significant revision.

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“…40 Over the last decades, increasing evidence has uncovered the underlying mechanisms involved in tumorigenesis and progression of pRCC, and it was gradually acknowledged that alternation in MET pathway was the main cause of type 1, whereas type 2 was more related to activation of the F I G U R E 8 Construction of SF-AS correlation network in pRCC. Moreover, KEGG analysis also brought us some novel clues to further elucidate cancer hallmarks related to pRCC, including autophagy, ErbB signaling pathway, PPAR signaling pathway, and AMPK signaling pathway, which were proved to have close relationship with anchorage-independent growth, 45 cell proliferation, membrane protein driving as well as cell migration 46 of pRCC. The yellow diamonds represent the prognostic SFs.…”

Section: Discussionmentioning

confidence: 99%

Identification of novel prognostic alternative splicing signature in papillary renal cell carcinoma

Duan

Zhang

2019

J of Cellular Biochemistry

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Papillary renal cell carcinoma (pRCC) is a heterogeneous disease containing multifocal or solitary tumors with an aggressive phenotype. Increasing evidence has indicated the involvement of aberrant splicing variants in renal cell cancer, while systematic profiling of aberrant alternative splicing (AS) in pRCC was lacking and largely unknown. In the current study, comprehensive profiling of AS events were performed based on the integration of pRCC cohort from the Cancer Genome Atlas database and SpliceSeq software. With rigorous screening and univariate Cox analysis, a total of 2077 prognoses AS events from 1642 parent genes were identified. Then, stepwise least absolute shrinkage and selection operator method‐penalized Cox regression analyses with 10‐fold cross‐validation followed by multivariate Cox regression were used to construct the prognostic AS signatures within each AS type. And a final 21 AS event‐based signature was proposed which showed potent prognostic capability in stratifying patients into low‐ and high‐risk subgroups (P < .0001). Furthermore, time‐dependent receiver operating characteristics curves confirmed that the final AS signature was effective and robust in predicting overall survival for pRCC patients with the area under the curve above 0.9 from 1 to 5 years. In addition, splicing correlation network was built to uncover the potential regulatory pattern among prognostic splicing factors and candidate AS events. Besides, gene set enrichment analysis revealed the involvement of these candidates AS events in tumor‐related pathways including extracellular matrix organization, oxidative phosphorylation, and P53 signaling pathways. Taken together, our results could contribute to elucidating the underlying mechanism of AS in the oncogenesis process and broaden the novel field of prognostic and clinical application of molecule‐targeted approaches in pRCC.

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COMMD5/HCaRG Hooks Endosomes on Cytoskeleton and Coordinates EGFR Trafficking

Cited by 22 publications

References 47 publications

Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling

Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling

Towards a molecular understanding of endosomal trafficking by Retromer and Retriever

Identification of novel prognostic alternative splicing signature in papillary renal cell carcinoma

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