prikaz prve stranice dokumenta Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism
Access restricted to all Croatian higher education institution's students and staff
Scientific paper - Original scientific paper
Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism
Nature Microbiology, 5 (2019), 2; 331-342. https://doi.org/10.1038/s41564-019-0624-1
Muscolino, Elena; Schmitz, Rebekka; Loroch, Stefan; Caragliano, Enrico; Schneider, Carola; Rizzato, Matteo; Kim, Young-Hyun; Krause, Eva; Juranić Lisnić, Vanda; Sickmann, Albert; Reimer, Rudolph; Ostermann, Eleonore; Brune, Wolfram

Institutional repository: Repository of the University of Rijeka, Faculty of Medicine

Cite this document

Muscolino, E., Schmitz, R., Loroch, S., Caragliano, E., Schneider, C., Rizzato, M. ... Brune, W. (2019). Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism. Nature Microbiology, 5. (2), 331-342. doi: 10.1038/s41564-019-0624-1

Muscolino, Elena, et al. "Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism." Nature Microbiology, vol. 5, no. 2, 2019, pp. 331-342. https://doi.org/10.1038/s41564-019-0624-1

Muscolino, Elena, Rebekka Schmitz, Stefan Loroch, Enrico Caragliano, Carola Schneider, Matteo Rizzato, Young Hyun Kim, et al. "Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism." Nature Microbiology 5, no. 2 (2019): 331-342. https://doi.org/10.1038/s41564-019-0624-1

Muscolino, E., et al. (2019) 'Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism', Nature Microbiology, 5(2), pp. 331-342. doi: 10.1038/s41564-019-0624-1

Muscolino E, Schmitz R, Loroch S, Caragliano E, Schneider C, Rizzato M, and sur.. Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism. Nature Microbiology [Internet]. 2019 [cited 2024 July 13];5(2):331-342. doi: 10.1038/s41564-019-0624-1

E. Muscolino, et al., "Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism", Nature Microbiology, vol. 5, no. 2, pp. 331-342, 2019. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:537367. [Accessed: 13 July 2024]

Metadata
Title (english)Herpesviruses induce aggregation and selective autophagy of host signalling proteins NEMO and RIPK1 as an immune-evasion mechanism
AuthorElena Muscolino
AuthorRebekka Schmitz
AuthorStefan Loroch
AuthorEnrico Caragliano
AuthorCarola Schneider
AuthorMatteo Rizzato
AuthorYoung-Hyun Kim
AuthorEva Krause
AuthorVanda Juranić Lisnić
AuthorAlbert Sickmann
AuthorRudolph Reimer
AuthorEleonore Ostermann
AuthorWolfram Brune
Author's institutionUniversity of Rijeka
Faculty of Medicine
(Center for Proteomics)
Author's institutionUniversity of Rijeka
Faculty of Medicine
(Department of Histology and Embryology)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
Viruses manipulate cellular signalling by inducing the degradation of crucial signal transducers, usually via the ubiquitin-proteasome pathway. Here, we show that the murine cytomegalovirus (Murid herpesvirus 1) M45 protein induces the degradation of two cellular signalling proteins, the nuclear factor κ-light- chain-enhancer of activated B cells (NF-κB) essential modulator (NEMO) and the receptor- interacting protein kinase 1 (RIPK1), via a different mechanism: it induces their sequestration as insoluble protein aggregates and subsequently facilitates their degradation by autophagy. Aggregation of target proteins requires a distinct sequence motif in M45, which we termed 'induced protein aggregation motif'. In a second step, M45 recruits the retromer component vacuolar protein sorting 26B (VPS26B) and the microtubule-associated protein light chain 3 (LC3)-interacting adaptor protein TBC1D5 to facilitate degradation of aggregates by selective autophagy. The induced protein aggregation motif is conserved in M45-homologous proteins of several human herpesviruses, including herpes simplex virus, Epstein-Barr virus and Kaposi's sarcoma-associated herpesvirus, but is only partially conserved in the human cytomegalovirus UL45 protein. We further show that the HSV-1 ICP6 protein induces RIPK1 aggregation and degradation in a similar fashion to M45. These data suggest that induced protein aggregation combined with selective autophagy of aggregates (aggrephagy) represents a conserved viral immune-evasion mechanism.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleNature Microbiology
Numberingvol. 5, no. 2, pp. 331-342
e-ISSN2058-5276
DOIhttps://doi.org/10.1038/s41564-019-0624-1
URN:NBNurn:nbn:hr:184:537367
Publication2019
Document URLhttp://bib.irb.hr/1093304
Type of resourceText
Access conditionsRestricted access
Terms of useLicence In copyright icon
Created on2022-02-22 07:36:30