A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-κB degradation and cell growth suppression in neuroblastoma

Mu, Ping; Akashi, Tomohiro; Lu, Fangjin; Kishida, Satoshi; Kadomatsu, Kenji

doi:10.1038/onc.2017.181

Cited by 31 publications

(29 citation statements)

References 58 publications

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“…It is also known as Tohoku University cDNA clone A on chromosome 3 (TU3A) or Family with sequence similarity 107, member A (FAM107A) [24,25]. DRR1 is downregulated in various cancer cell lines, including renal cell, ovarian, cervical, laryngeal, gastric, prostate, liver, lymph, and non-small cell lung cancer and is associated with the progression of neuroblastoma, meningioma and malignant glioma [26,27,28,29,30,31,32,33,34,35,36]. On the other hand, DRR1 is highly expressed in outer radial glial cells [37] and in the invasive component of glioblastoma [38,39].…”

Section: Introductionmentioning

confidence: 99%

The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics

Kretzschmar

Schülke

Masana

et al. 2018

IJMS

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Cytoskeletal dynamics are pivotal to memory, learning, and stress physiology, and thus psychiatric diseases. Downregulated in renal cell carcinoma 1 (DRR1) protein was characterized as the link between stress, actin dynamics, neuronal function, and cognition. To elucidate the underlying molecular mechanisms, we undertook a domain analysis of DRR1 and probed the effects on actin binding, polymerization, and bundling, as well as on actin-dependent cellular processes. Methods: DRR1 domains were cloned and expressed as recombinant proteins to perform in vitro analysis of actin dynamics (binding, bundling, polymerization, and nucleation). Cellular actin-dependent processes were analyzed in transfected HeLa cells with fluorescence recovery after photobleaching (FRAP) and confocal microscopy. Results: DRR1 features an actin binding site at each terminus, separated by a coiled coil domain. DRR1 enhances actin bundling, the cellular F-actin content, and serum response factor (SRF)-dependent transcription, while it diminishes actin filament elongation, cell spreading, and actin treadmilling. We also provide evidence for a nucleation effect of DRR1. Blocking of pointed end elongation by addition of profilin indicates DRR1 as a novel barbed end capping factor. Conclusions: DRR1 impacts actin dynamics in several ways with implications for cytoskeletal dynamics in stress physiology and pathophysiology.

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Section: Introductionmentioning

confidence: 99%

The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics

Kretzschmar

Schülke

Masana

et al. 2018

IJMS

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“…Actin interaction with nuclear DNA helicase II (NDH II), also designated RNA helicase A, is direct and promotes attachment of nuclear ribonucleoprotein complexes to filamentous actin [246]. Actin can also bind to a tumor suppressor, down-regulated in renal cell carcinoma 1 (DRR1) [247,248]. Since actin is one of the most abundant, if not the most abundant eukaryotic protein, it is not surprising that mutations in ACTB genes are linked to numerous diseases, such as dystonia, juvenile-onset (DJO) [249], Baraitser–Winter syndrome 1 (BRWS1) [250], inherited myopathy [251], combined and complex dystonia [252], developmental malformations–deafness–dystonia syndrome, as well as multiple tumors, such as melanoma, blastoma, and hematologic, lung, urinary, uterine, bladder, kidney, and colorectal cancers.…”

Section: Resultsmentioning

confidence: 99%

Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development

Hadidy

Uversky

2019

IJMS

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The two-meter-long DNA is compressed into chromatin in the nucleus of every cell, which serves as a significant barrier to transcription. Therefore, for processes such as replication and transcription to occur, the highly compacted chromatin must be relaxed, and the processes required for chromatin reorganization for the aim of replication or transcription are controlled by ATP-dependent nucleosome remodelers. One of the most highly studied remodelers of this kind is the BRG1- or BRM-associated factor complex (BAF complex, also known as SWItch/sucrose non-fermentable (SWI/SNF) complex), which is crucial for the regulation of gene expression and differentiation in eukaryotes. Chromatin remodeling complex BAF is characterized by a highly polymorphic structure, containing from four to 17 subunits encoded by 29 genes. The aim of this paper is to provide an overview of the role of BAF complex in chromatin remodeling and also to use literature mining and a set of computational and bioinformatics tools to analyze structural properties, intrinsic disorder predisposition, and functionalities of its subunits, along with the description of the relations of different BAF complex subunits to the pathogenesis of various human diseases.

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“…Because some participants of CTS are still unknown while some copper-binding proteins are 'moonlighting' and their activities dependent on copper level (e.g. Cp, CTR1, ATOX1, COMMD1) [31,[151][152][153][154][155], we may suggest that the differences between breastmilk and infant formulas with respect to copper concentrations and copper 'packaging' by the Cp protein may be one of the factors that contribute to the negative effects of bottle feeding on the cognitive abilities of children [156,157].…”

Section: Resultsmentioning

confidence: 99%

Copper Metabolism of Newborns Is Adapted to Milk Ceruloplasmin As a Nutritive Source of Copper

Puchkova¹,

Babich²,

Zatulovskaia³

et al. 2018

Preprint

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Copper, which can potentially be a highly toxic agent, is an essential nutrient due to its role as a co-factor for cuproenzymes and participation in signaling pathways. In mammals, the liver is a central organ that controls copper turnover throughout the body: copper absorption, distribution, and excretion. In ontogenesis, there are two types of copper metabolism: embryonic and adult, which maintain the balance of copper in each of these periods, respectively. In the liver cells, these types are characterized by specific expression patterns and activity levels of the genes encoding ceruloplasmin, which is the main extracellular ferroxidase and copper transporter and proteins mediating ceruloplasmin metalation. In newborns, the molecular-genetic mechanisms responsible for copper homeostasis and the ontogenetic switch from embryonic to adult copper metabolism are highly adapted to milk ceruloplasmin as a dietary source of copper. In the mammary gland cells, the level of ceruloplasmin gene expression and the alternative splicing of its pre-mRNA govern the amount of ceruloplasmin in milk, and thus, the amount of copper absorbed by the newborn is controlled. In the newborns, absorption, distribution, and accumulation copper are adapted to milk ceruloplasmin. In the newborns, which are not breast-fed at the early stages of postnatal development, the control for alimentary copper balance is absent. We tried to focus on the neonatal consequences of a violation of the balance of copper in the mother / newborn system. Although there is still much to be learned, the time to pay attention to this problem came because the neonatal misbalance of copper may provoke the development of copper related disorders for future life.

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A novel nuclear complex of DRR1, F-actin and COMMD1 involved in NF-κB degradation and cell growth suppression in neuroblastoma

Cited by 31 publications

References 58 publications

The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics

The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics

Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development

Copper Metabolism of Newborns Is Adapted to Milk Ceruloplasmin As a Nutritive Source of Copper

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