Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Woznik, Maria; Rödner, Claudia; Lemon, Ken; Rima, B. K.; Mankertz, Annette; Finsterbusch, Tim

doi:10.1099/vir.0.024638-0

Cited by 17 publications

(14 citation statements)

References 29 publications

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“…Yeast two-hybrid mapping indicate that the interacting region of ubiquilin-1 comprised the STI-1-like motifs located at the central region of the protein; a role for ubiquilin-1 in regulating the assembly and trafficking of nAChR has been proposed [62]. The small hydrophobic (SH) protein of mumps virus (MuV) interacts with the ataxin-1 ubiquitin-like interacting protein (A1Up, ubiquilin-4), and this interaction is mediated by the central region of A1Up; the role of this interaction during MuV infection is unknown [63]. A complex that includes the interaction between erasin, a protein that prompts ERAD, and ubiquilin-1 has also been reported; this interaction is mediated by the central region of ubiquilin-1.…”

Section: Discussionmentioning

confidence: 99%

Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments

2011

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Ubiquitin-ligases or E3s are components of the ubiquitin proteasome system (UPS) that coordinate the transfer of ubiquitin to the target protein. A major class of ubiquitin-ligases consists of RING-finger domain proteins that include the substrate recognition sequences in the same polypeptide; these are known as single-subunit RING finger E3s. We are studying a particular family of RING finger E3s, named ATL, that contain a transmembrane domain and the RING-H2 finger domain; none of the member of the family contains any other previously described domain. Although the study of a few members in A. thaliana and O. sativa has been reported, the role of this family in the life cycle of a plant is still vague. To provide tools to advance on the functional analysis of this family we have undertaken a phylogenetic analysis of ATLs in twenty-four plant genomes. ATLs were found in all the 24 plant species analyzed, in numbers ranging from 20–28 in two basal species to 162 in soybean. Analysis of ATLs arrayed in tandem indicates that sets of genes are expanding in a species-specific manner. To get insights into the domain architecture of ATLs we generated 75 pHMM LOGOs from 1815 ATLs, and unraveled potential protein-protein interaction regions by means of yeast two-hybrid assays. Several ATLs were found to interact with DSK2a/ubiquilin through a region at the amino-terminal end, suggesting that this is a widespread interaction that may assist in the mode of action of ATLs; the region was traced to a distinct sequence LOGO. Our analysis provides significant observations on the evolution and expansion of the ATL family in addition to information on the domain structure of this class of ubiquitin-ligases that may be involved in plant adaptation to environmental stress.

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Section: Discussionmentioning

confidence: 99%

Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments

2011

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“…This interaction was found to promote the degradation of both p53 and the NF-B inhibitor IB and to protect cells from apoptosis. More recently, another small hydrophobic protein from mumps virus named SH was also reported to interact with both UBQLN1 and UBQLN4 (57). This interaction relocalized SH to punctate structures positive for proteosomal markers, but the functional role of this interaction remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Mapping of Chikungunya Virus Interactions with Host Proteins Identified nsP2 as a Highly Connected Viral Component

Bouraï

Lucas‐Hourani

Gad

et al. 2012

J Virol

102

111

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h Chikungunya virus (CHIKV) is a mosquito-transmitted alphavirus that has been responsible for an epidemic outbreak of unprecedented magnitude in recent years. Since then, significant efforts have been made to better understand the biology of this virus, but we still have poor knowledge of CHIKV interactions with host cell components at the molecular level. Here we describe the extensive use of high-throughput yeast two-hybrid (HT-Y2H) assays to characterize interactions between CHIKV and human proteins. A total of 22 high-confidence interactions, which essentially involved the viral nonstructural protein nsP2, were identified and further validated in protein complementation assay (PCA). These results were integrated to a larger network obtained by extensive mining of the literature for reports on alphavirus-host interactions. To investigate the role of cellular proteins interacting with nsP2, gene silencing experiments were performed in cells infected by a recombinant CHIKV expressing Renilla luciferase as a reporter. Collected data showed that heterogeneous nuclear ribonucleoprotein K (hnRNP-K) and ubiquilin 4 (UBQLN4) participate in CHIKV replication in vitro. In addition, we showed that CHIKV nsP2 induces a cellular shutoff, as previously reported for other Old World alphaviruses, and determined that among binding partners identified by yeast twohybrid methods, the tetratricopeptide repeat protein 7B (TTC7B) plays a significant role in this activity. Altogether, this report provides the first interaction map between CHIKV and human proteins and describes new host cell proteins involved in the replication cycle of this virus.

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“…5D, left). 22 Likewise, 361 out of the 1214 mapped VTPs showed direct interactions with 2 or more EHFs and 12 VTPs showed direct interactions with 15 or more EHFs, including YWHAG, CTNNB1, PIK3R1, YWHAZ, YWHAB, TRAF2, UBE2I, CAV1, CDK1, VIM, CRK, and RAC1 (Fig. Yamaguchi et al have proved that a shift of SMAD3 phospho-isoform signaling from tumor suppression to carcinogenesis increases the risk of hepatocellular carcinoma in the hepatitis C virus (HCV) infection.…”

Section: Ehfs and Vtps In The Human Ppi Networkmentioning

confidence: 99%

Exploring the associations of host genes for viral infection revealed by genome-wide RNAi and virus–host protein interactions

et al. 2015

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Genome-wide RNA interference screens have greatly facilitated the identification of essential host factors (EHFs) for viral infections, whose knockdown effects significantly influence virus replication but not host cell viability. However, little has been done to link EHFs with another important host factor type, i.e., virus targeting proteins (VTPs) that viruses directly interact with for intracellular survival, hampering the integrative understanding of virus-host interactions. Using EHFs and VTPs for human immunodeficiency virus type 1 (HIV-1) and influenza A virus (IAV) infections, we found in general that despite limited overlap, EHFs and VTPs are both among the most differentially dysregulated genes in host transcriptional response to HIV and IAV infections, and notably they show consistency in regulation orientation. In the human protein-protein interaction network, both EHFs and VTPs hold topologically important positions at the global center, and importantly their direct interactions are statistically significant. We also identified BRCA1 and TP53 (or SMAD3 and PIK3R1) being the most extensive VTP-interacting EHFs (or EHF-interacting VTPs) for HIV-1 and IAV, which hold great potential in deciphering specific infection features and discovery of host directed antivirals. Further, most EHFs are the upstream regulators of VTPs when mapped in the same signaling pathways, some of which present intensive cross links. Collectively, these results provide insights into functional associations of the identified host gene factors for viral infections and highlight the regulatory significance of EHFs, and the necessity of their selective exploitation in confrontation to viral infections.

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Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)

Cited by 17 publications

References 29 publications

Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments

Diversity in the Architecture of ATLs, a Family of Plant Ubiquitin-Ligases, Leads to Recognition and Targeting of Substrates in Different Cellular Environments

Mapping of Chikungunya Virus Interactions with Host Proteins Identified nsP2 as a Highly Connected Viral Component

Exploring the associations of host genes for viral infection revealed by genome-wide RNAi and virus–host protein interactions

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