Characterization of nuclear import and export signals determining the subcellular localization of WD repeat‐containing protein 42A (WDR42A)

Wu, Fuqing; Wang, Shuai; Xing, Junji; Li, Meili; Zheng, Chunfu

doi:10.1016/j.febslet.2012.02.053

Cited by 8 publications

(6 citation statements)

References 35 publications

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“…Mutations in DCAF8 (R314H or R362H) decreased the binding of DCAF8 to DDB1 (Angers et al, 2006) but did not affect its binding to H3 ( Figure 2D). Additionally, DCAF8, which is mostly located in the nucleus by immunofluorescent microscopy (Wu et al, 2012; Figure S2C), associated with H3 on chromatin in 293T cells ( Figure 2E) and (C) Western blot analysis for ubiquitin immunoprecipitated with anti-H3 antibody in chromatin fractionations prepared from two mice hepatocytes. Mock immunoprecipitation with immunoglobulin G (IgG) was shown.…”

Section: Chromatin-bound Histone H3 Is Ubiquitinated By Crl4 In Adultmentioning

confidence: 98%

CRL4DCAF8 Ubiquitin Ligase Targets Histone H3K79 and Promotes H3K9 Methylation in the Liver

Chen

et al. 2017

Cell Reports

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Transcription from chromosomes is regulated by posttranslational modifications to histones, such as methylation and ubiquitination. Monoubiquitination of histones H2A and H2B influences H3 methylation to reinforce the activation or repression of gene expression. Here, we provide evidence that H3 polyubiquitination represses transcription of fetal and cell-cycle genes in postnatal mouse liver by crosstalk with H3K9 methylation. We found that the CRL4 ubiquitin ligase targets H3 for polyubiquitination at K79 via the DCAF8 substrate receptor in hepatocytes. Genetic inactivation of DCAF8 and overexpression of an H3K79 mutant in cells or inducible deletion of CRL4 in mouse liver abrogates H3 ubiquitination, reactivates the expression of fetal liver and cell-cycle genes by interfering with methylated H3K9 occupancy, and leads to cell senescence. Restoring CRL4 expression in cells with decreased H3 ubiquitination reinstates the epigenetic gene silencing. Our results suggest that progressive H3 ubiquitination plays an important role in postnatal liver maturation.

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Section: Chromatin-bound Histone H3 Is Ubiquitinated By Crl4 In Adultmentioning

confidence: 98%

CRL4DCAF8 Ubiquitin Ligase Targets Histone H3K79 and Promotes H3K9 Methylation in the Liver

Chen

et al. 2017

Cell Reports

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“…6E). Gene11150 codes for an F-box/Kelch-repeat protein, gene32754 encodes a WD repeat-containing protein 42A, which interacts with Cullin4-Damage-specific DNA-binding protein1 (Ddb1) E3 ligase and is a nucleocytoplasmic shuttling protein (Wu et al, 2012), gene07916 is a homolog of 26S protease regulatory subunit 4, gene01189 encodes histone 3.3, and gene20570 encodes an aspartic proteinase (precursor of nepenthesin1). The identity of these hub genes underscores active protein degradation activities during stage 9 anther development.…”

Section: Anther Stage 9-specific Module Transiently Expresses a Largementioning

confidence: 99%

Floral Transcriptomes in Woodland Strawberry Uncover Developing Receptacle and Anther Gene Networks

et al. 2014

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ORCID IDs: 0000-0002-6902-740X (C.K.); 0000-0001-9969-9381 (Z.L.).Flowers are reproductive organs and precursors to fruits and seeds. While the basic tenets of the ABCE model of flower development are conserved in angiosperms, different flowering plants exhibit different and sometimes unique characteristics. A distinct feature of strawberry (Fragaria spp.) flowers is the development of several hundreds of individual apocarpous (unfused) carpels. These individual carpels are arranged in a spiral pattern on the subtending stem tip, the receptacle. Therefore, the receptacle is an integral part of the strawberry flower and is of significant agronomic importance, being the precursor to strawberry fruit. Taking advantage of next-generation sequencing and laser capture microdissection, we generated different tissue-and stage-transcriptomic profiling of woodland strawberry (Fragaria vesca) flower development. Using pairwise comparisons and weighted gene coexpression network analysis, we identified modules of coexpressed genes and hub genes of tissue-specific networks. Of particular importance is the discovery of a developing receptacle-specific module exhibiting similar molecular features to those of young floral meristems. The strawberry homologs of a number of meristem regulators, including LOST MERISTEM and WUSCHEL, are identified as hub genes operating in the developing receptacle network. Furthermore, almost 25% of the F-box genes in the genome are transiently induced in developing anthers at the meiosis stage, indicating active protein degradation. Together, this work provides important insights into the molecular networks underlying strawberry's unique reproductive developmental processes. This extensive floral transcriptome data set is publicly available and can be readily queried at the project Web site, serving as an important genomic resource for the plant biology research community.

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“…To further verify the nuclear import mechanism, co-immunoprecipitation (Co-IP) assays were performed as described previously (Cai et al , 2012; Wu et al , 2012; Xing et al , 2011a). The results show that Flag-importin β1 was co-immunoprecipitated with VP19C-HA but not Flag-importin α5, whereas no such protein was immunoprecipitated with control IgG or HA-vector control ().…”

Section: Full Textmentioning

confidence: 99%

Identification of a novel NLS of herpes simplex virus type 1 (HSV-1) VP19C and its nuclear localization is required for efficient production of HSV-1

Zhao

Wang

et al. 2012

Journal of General Virology

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Herpes simplex virus type 1 (HSV-1) triplex is a complex of three protein subunits, consisting of two copies of VP23 and one copy of VP19C. Here, we identified a non-classical NLS of VP19C between aa 50 and 61, and the nuclear import of VP19C was mediated by RanGTP and importin b1-, but not importin a5-, dependent pathway. Additionally, recombinant virus harbouring this NLS mutation (NLSm) replicates less efficiently as wild-type. These data strongly suggested that the nuclear import of VP19C is required for efficient HSV-1 production.Herpes simplex virus type 1 (HSV-1), a typical alphaherpesvirus, causes a spectrum of diseases, including herpes labialis, herpes keratitis and herpes encephalitis, which can be lethal . VP19C is a structural protein of the HSV-1 viral particle, which forms a triplex consisting of two copies of VP23 and one copy of VP19C (Chowdhury & Batterson, 1994;Kim et al., 2011;Solé et al., 2007;Spencer et al., 1998). There are 320 hetero-trimeric triplex molecules per capsid, which are assembled in the cytoplasm and transported to the nucleus, where higherorder capsid shells are assembled (Okoye et al., 2006;Saad, 2003;Solé et al., 2007;Trus et al., 1996). VP19C is essential for assembly of the capsid and if it is absent capsid shells do not form (Person & Desai, 1998). A previous report has described that the nuclear targeting property of VP19C is required for nuclear transport of VP23 (Rixon et al., 1996), which is incapable of localizing to the nucleus on its own. A previous study has demonstrated that the N terminus of VP19C was required for its nuclear import (Adamson et al., 2006); however, the precise NLS responsible for its nuclear targeting was still elusive.As previously reported (Rixon et al., 1996), VP19C exhibited a predominantly, if not exclusively, nuclear localization in HSV-1-infected cells, which was demonstrated by using a fixation procedure. However, it is well known that some fixation protocols may alter the subcellular localization of proteins, resulting in misleading conclusions. As an alternative method to investigate the intracellular distribution of VP19C, a living-cell fluorescence microscopy technique and enhanced-yellow-fluorescent protein (EYFP)-tagged variants were applied (Cai et al., 2011;Xing et al., 2010 Xing et al., , 2011b. To investigate the subcellular localization of VP19C in the absence of other viral proteins, pVP19C-EYFP was constructed and transfected into COS-7 cells as described previously (Li et al., 2011a). The fluorescence of VP19C-EYFP was predominantly restricted to the nucleus (Fig. 1c), which is consistent with the previous report (Rixon et al., 1996).It was previously reported that the first 56 aa of VP19C was important for its nuclear localization (Adamson et al., 2006); however, the precise NLS was still unknown. To map the amino acid sequence within VP19C responsible for its nuclear localization, a series of deletion mutants encompassing aa 1-30, 30-50, 41-52, 50-61 and 1-61 each fused to EYFP were constructed (Fig. 1a). Their expressi...

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Characterization of nuclear import and export signals determining the subcellular localization of WD repeat‐containing protein 42A (WDR42A)

Cited by 8 publications

References 35 publications

CRL4DCAF8 Ubiquitin Ligase Targets Histone H3K79 and Promotes H3K9 Methylation in the Liver

CRL4DCAF8 Ubiquitin Ligase Targets Histone H3K79 and Promotes H3K9 Methylation in the Liver

Floral Transcriptomes in Woodland Strawberry Uncover Developing Receptacle and Anther Gene Networks

Identification of a novel NLS of herpes simplex virus type 1 (HSV-1) VP19C and its nuclear localization is required for efficient production of HSV-1

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