COMMD proteins: COMMing to the scene

Maine, Gabriel N.; Burstein, Ezra

doi:10.1007/s00018-007-7078-y

Cited by 97 publications

(104 citation statements)

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“…In all of these cases, the mechanism of action of COMMD1 in facilitating protein degradation can be unified by its involvement in the ubiquitin-proteasome pathway (35)(36)(37). The action of COMMD1 in facilitating the degradation of ATP7B via the proteasomal pathway is consistent with this.…”

Section: Discussionmentioning

confidence: 53%

“…This, together with its interaction with the ATP7B N terminus, subcellular localization pattern, and the canine copper toxicosis phenotype, led to the suggestion of a role for COMMD1 in regulating ATP7B-mediated biliary copper excretion (16,35). More recently, COMMD1 was shown to bind more strongly to the ATP7B N terminus, which harbored certain WD-causing mutations that rendered the protein less stable than WT-ATP7B (17).…”

Section: Discussionmentioning

confidence: 99%

“…However, more recent data has implicated COMMD1 in a variety of cellular processes and signaling pathways (35). The data in all cases, point to a general role of COMMD1 in controlling protein degradation and stability (35)(36)(37).…”

mentioning

confidence: 96%

“…The COMMD1 gene was found to be deleted in Bedlington terrier dogs that exhibit canine copper toxicosis, a chronic liver copper overload disease that resembles WD (33). However, more recent data has implicated COMMD1 in a variety of cellular processes and signaling pathways (35). The data in all cases, point to a general role of COMMD1 in controlling protein degradation and stability (35)(36)(37).…”

mentioning

confidence: 99%

“…COMMD1 is a member of the COMMD (copper metabolism Murr1 domain) family of proteins that share a highly conserved C-terminal COMM domain (35). All of the COMMD proteins interact with each other via the COMM domains.…”

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confidence: 99%

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Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

Materia

Cater

Klomp³

et al. 2012

Journal of Biological Chemistry

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Background: Clusterin and COMMD1 interact to down-regulate copper transporters ATP7A and ATP7B. Results: Clusterin and COMMD1 act independently and under different conditions to target ATP7B degradation via different pathways. Conclusion: Clusterin and COMMD1 regulate the quality control of ATP7A/ATP7B and directly impact copper homeostasis. Significance: Clusterin and COMMD1 allelic variations may influence the clinical expression of Menkes and Wilson diseases.

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Section: Discussionmentioning

confidence: 53%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 96%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

Materia

Cater

Klomp³

et al. 2012

Journal of Biological Chemistry

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Multi‐omics analysis of the oncogenic value of copper Metabolism‐Related protein COMMD2 in human cancers

et al. 2022

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Background The copper metabolism MURR1 domain (COMMD) protein family is involved in tumorigenicity of malignant tumors. However, as the member of COMMD, the role of COMMD2 in human tumors remains unknown. Methods We used The Cancer Genome Atlas (TCGA), Genotype Tissue Expression (GTEx), Human Protein Atlas (HPA) database, Cancer Cell Line Encyclopedia (CCLE) platform, univariate Cox regression analysis, Kaplan–Meier curve, cBioPortal, UALCAN database, Sangerbox online platform, GSCA database gene set enrichment analysis (GSEA), and GeneMANIA to analyze the expression of COMMD2, its prognostic values, genomic alteration patterns, and the correlation with tumor stemness, tumor mutational burden (TMB), microsatellite instability (MSI), and immune infiltrates, drug sensitivity, and gene function enrichment in pan‐cancer. qRT‐PCR, CCK‐8, EdU, wound healing, and transwell migration assays were performed to confirm the function of COMMD2. Results COMMD2 was strongly expressed in most cancer types. Elevated COMMD2 expression affects the prognosis, clinicopathological stage, and molecular or immune subtypes of various tumors. Moreover, promoter hypomethylation and mutations in the COMMD2 gene may be associated with its high expression and poor survival. Additionally, we discovered that COMMD2 expression was linked to tumor stemness, TMB, MSI, immune cell infiltration, immune‐checkpoint inhibitors, and drug sensitivity in pan‐cancer. Furthermore, the COMMD2 gene co‐expression network is constructed with GSEA analysis, displaying significant interaction of COMMD2 with E2F targets, G2‐M checkpoint, and mitotic spindle in bladder cancer (BLCA). Finally, RNA interference data showed suppression of COMMD2 prevented proliferation and migration of BLCA and uterine corpus endometrial carcinoma (UCEC) cells. Conclusion Our findings shed light on the COMMD2 functions in human cancers and demonstrate that it is a promising prognostic biomarker and therapeutic target in pan‐cancer.

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Intersection of Iron and Copper Metabolism in the Mammalian Intestine and Liver

Doguer

Collins

2018

Comprehensive Physiology

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Iron and copper have similar physiochemical properties; thus, physiologically relevant interactions seem likely. Indeed, points of intersection between these two essential trace minerals have been recognized for many decades, but mechanistic details have been lacking. Investigations in recent years have revealed that copper may positively influence iron homeostasis, and also that iron may antagonize copper metabolism. For example, when body iron stores are low, copper is apparently redistributed to tissues important for regulating iron balance, including enterocytes of upper small bowel, the liver, and blood. Copper in enterocytes may positively influence iron transport, and hepatic copper may enhance biosynthesis of a circulating ferroxidase, ceruloplasmin, which potentiates iron release from stores. Moreover, many intestinal genes related to iron absorption are transactivated by a hypoxia-inducible transcription factor, hypoxia-inducible factor-2α (HIF2α), during iron deficiency. Interestingly, copper influences the DNA-binding activity of the HIF factors, thus further exemplifying how copper may modulate intestinal iron homeostasis. Copper may also alter the activity of the iron-regulatory hormone hepcidin. Furthermore, copper depletion has been noted in iron-loading disorders, such as hereditary hemochromatosis. Copper depletion may also be caused by high-dose iron supplementation, raising concerns particularly in pregnancy when iron supplementation is widely recommended. This review will cover the basic physiology of intestinal iron and copper absorption as well as the metabolism of these minerals in the liver. Also considered in detail will be current experimental work in this field, with a focus on molecular aspects of intestinal and hepatic iron-copper interplay and how this relates to various disease states. © 2018 American Physiological Society. Compr Physiol 8:1433-1461, 2018.

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COMMD proteins: COMMing to the scene

Cited by 97 publications

References 50 publications

Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

Multi‐omics analysis of the oncogenic value of copper Metabolism‐Related protein COMMD2 in human cancers

Intersection of Iron and Copper Metabolism in the Mammalian Intestine and Liver

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