Overexpression of CIN85 suppresses the growth of herpes simplex virus in HeLa cells

Narita, Toyoko; Andõ, Akira; Mikami, Yuzuru; Taniyama, Tadayoshi

doi:10.1016/j.yexcr.2005.09.007

Experimental Cell Research

2005

DOI: 10.1016/j.yexcr.2005.09.007

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Overexpression of CIN85 suppresses the growth of herpes simplex virus in HeLa cells

Toyoko Narita

Akira Andõ

Yuzuru Mikami

et al.

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Cited by 5 publications

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“…Ruk/CIN85 appears to behave in a similar way. A growing body of evidence suggests that Ruk/CIN85 is required for the regulation of different cellular processes including signal transduction (1,6–9), vesicle‐mediated transport (10–15), cytoskeleton remodelling (16–19), programmed cell death (1,8,20,21) and viral infection (22,23).…”

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confidence: 99%

Emerging Roles of Ruk/CIN85 in Vesicle-Mediated Transport, Adhesion, Migration and Malignancy

Havrylov

Redowicz

Buchman

2010

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Ruk/CIN85 is an adaptor protein. Similar to many other proteins of this type, Ruk/CIN85 is known to take part in multiple cellular processes including signal transduction, vesicle-mediated transport, cytoskeleton remodelling, programmed cell death and viral infection. Recent studies have also revealed the potential importance of Ruk/CIN85 in cancer cell invasiveness. In this review we summarize the various roles of this protein as well as the potential contribution of Ruk/CIN85 to malignancy and the invasiveness of cancer cells. In the last section of the paper we also speculate on the utility of Ruk/CIN85 as a target for novel anti-cancer therapies.

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confidence: 99%

Emerging Roles of Ruk/CIN85 in Vesicle-Mediated Transport, Adhesion, Migration and Malignancy

Havrylov

Redowicz

Buchman

2010

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Increased levels of the HER1 adaptor protein Ruk l /CIN85 contribute to breast cancer malignancy

et al. 2012

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The adaptor protein regulator for ubiquitous kinase/c-Cbl-interacting protein of 85kDa (Ruk/CIN85) was found to modulate HER1/EGFR signaling and processes like cell adhesion and apoptosis. Although these features imply a role in carcinogenesis, it is so far unknown how and by which molecular mechanisms Ruk/CIN85 could affect a certain tumor phenotype. By analyzing samples from breast cancer patients, we found high levels of Ruk(l)/CIN85 especially in lymph node metastases from patients with invasive breast adenocarcinomas, suggesting that Ruk(l)/CIN85 contributes to malignancy. Expression of Ruk(l)/CIN85 in weakly invasive breast adenocarcinoma cells deficient of Ruk(l)/CIN85 indeed converted them into more malignant cells. In particular, Ruk(l)/CIN85 reduced the growth rate, decreased cell adhesion, enhanced anchorage-independent growth, increased motility in both transwell migration and wound healing assays as well as affected the response to epidermal growth factor. Thereby, Ruk(l)/CIN85 led to a more rapid and prolonged epidermal growth factor-dependent activation of Src, Akt and ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk(l)/CIN85-dependent changes in cell motility. Together, this study indicates that high levels of Ruk(l)/CIN85 contribute to the conversion of breast adenocarcinoma cells into a more malignant phenotype via modulation of the Src/Akt pathway.

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Porcine reproductive and respiratory syndrome virus nonstructural protein 2 promotes the autophagic degradation of adaptor protein SH3KBP1 to antagonize host innate immune responses by enhancing K63-linked polyubiquitination of RIG-I

Li,

Zhang,

Sun

et al. 2024

PLoS Pathog

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Non-structural protein 2 (NSP2) of PRRSV is highly variable and plays crucial roles in the virus’s life cycle. To elucidate the function of NSP2 during PRRSV infection, we identified SH3KBP1 as an NSP2-interacting host protein using mass spectrometry. Exogenous SH3KBP1 expression significantly inhibited PRRSV replication by enhancing IFN-I and related ISGs production. Conversely, SH3KBP1 knockdown promoted viral replication by downregulating IFN-I and ISGs levels. In vivo experiments revealed that Sh3kbp1-/- mice were more susceptible to VSV infection, exhibiting reduced serum IFN-β levels. Further investigation showed that SH3KBP1 enhances RIG-I signal transduction by increasing K63-linked polyubiquitination through interaction with the E3 ubiquitin ligase TRIM25. We also found that PRRSV infection and NSP2 overexpression induce the autophagic degradation of SH3KBP1, counteracting the host’s innate immune response. A critical interaction site was identified within the third proline-rich motif in NSP2 (453PVPAPR458). Recombinant PRRSV lacking this motif displayed reduced virulence and decreased SH3KBP1 degradation. This study advances our understanding of how PRRSV interferes with the host immune response and offers valuable insights for development novel attenuated vaccines against PRRSV.

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Overexpression of CIN85 suppresses the growth of herpes simplex virus in HeLa cells

Cited by 5 publications

References 25 publications

Emerging Roles of Ruk/CIN85 in Vesicle-Mediated Transport, Adhesion, Migration and Malignancy

Emerging Roles of Ruk/CIN85 in Vesicle-Mediated Transport, Adhesion, Migration and Malignancy

Increased levels of the HER1 adaptor protein Ruk l /CIN85 contribute to breast cancer malignancy

Porcine reproductive and respiratory syndrome virus nonstructural protein 2 promotes the autophagic degradation of adaptor protein SH3KBP1 to antagonize host innate immune responses by enhancing K63-linked polyubiquitination of RIG-I

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