prikaz prve stranice dokumenta Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
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Scientific paper - Original scientific paper
Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
Journal of General Virology, 97 (2016), 7; 1676-1685. https://doi.org/10.1099/jgv.0.000495
Sonntag, Eric; Hamilton, Stuart T.; Bahsi, Hanife; Wagner, Sabrina; Jonjić, Stipan; Rawlinson, William D.; Marschall, Manfred; Milbradt, Jens

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

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Sonntag, E., Hamilton, S. T., Bahsi, H., Wagner, S., Jonjić, S., Rawlinson, W. D. ... Milbradt, J. (2016). Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components. Journal of General Virology, 97. (7), 1676-1685. doi: 10.1099/jgv.0.000495

Sonntag, Eric, et al. "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components." Journal of General Virology, vol. 97, no. 7, 2016, pp. 1676-1685. https://doi.org/10.1099/jgv.0.000495

Sonntag, Eric, Stuart T. Hamilton, Hanife Bahsi, Sabrina Wagner, Stipan Jonjić, William D. Rawlinson, Manfred Marschall and Jens Milbradt. "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components." Journal of General Virology 97, no. 7 (2016): 1676-1685. https://doi.org/10.1099/jgv.0.000495

Sonntag, E., et al. (2016) 'Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components', Journal of General Virology, 97(7), pp. 1676-1685. doi: 10.1099/jgv.0.000495

Sonntag E, Hamilton ST, Bahsi H, Wagner S, Jonjić S, Rawlinson WD, and sur.. Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components. Journal of General Virology [Internet]. 2016 July 01 [cited 2024 May 14];97(7):1676-1685. doi: 10.1099/jgv.0.000495

E. Sonntag, et al., "Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components", Journal of General Virology, vol. 97, no. 7, pp. 1676-1685, July 2016. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:757453. [Accessed: 14 May 2024]

Metadata
Title (english)Cytomegalovirus pUL50 is the multi-interacting determinant of the core nuclear egress complex (NEC) that recruits cellular accessory NEC components
AuthorEric Sonntag
AuthorStuart T. Hamilton
AuthorHanife Bahsi
AuthorSabrina Wagner
AuthorStipan Jonjić
AuthorWilliam D. Rawlinson
AuthorManfred Marschall
AuthorJens Milbradt
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 (croatian)
Nuclear egress of herpesvirus capsids through the nuclear envelope is mediated by the multimeric nuclear egress complex (NEC). The human cytomegalovirus (HCMV) core NEC is defined by an interaction between the membrane- anchored pUL50 and its nuclear co-factor pUL53, tightly associated through heterodimeric corecruitment to the nuclear envelope. Cellular proteins, such as p32/gC1qR, emerin and protein kinase C (PKC), are recruited by direct interaction with pUL50 for the multimeric extension of the NEC. As a functionally important event, the recruitment of both viral and cellular protein kinases leads to site- specific lamin phosphorylation and nuclear lamina disassembly. In this study, interaction domains within pUL50 for its binding partners were defined by co-immunoprecipitation. The interaction domain for pUL53 is located within the pUL50 N-terminus (residues 10-169), interaction domains for p32/gC1qR (100-358) and PKC (100-280) overlap in the central part of pUL50, and the interaction domain for emerin is located in the C-terminus (265-397). Moreover, expression and formation of core NEC proteins at the nuclear rim were consistently detected in cells permissive for productive HCMV replication, including two trophoblast-cell lines. Importantly, regular nuclear-rim formation of the core NEC was blocked by inhibition of cyclin-dependent kinase (CDK) activity. In relation to the recently published crystal structure of the HCMV core NEC, our findings result in a refined view of NEC assembly. In particular, we suggest that CDKs may play an important regulatory role in NEC formation during HCMV replica.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleJournal of General Virology
Numberingvol. 97, no. 7, pp. 1676-1685
p-ISSN0022-1317
e-ISSN1465-2099
DOIhttps://doi.org/10.1099/jgv.0.000495
URN:NBNurn:nbn:hr:184:757453
Publication2016-07-01
ProjectNumber: 062-0621261-1263
Title (croatian): Molekularni mehanizmi citomegalovirusnog izmicanja imunološkom nadzoru
Leader: Stipan Jonjić
Jurisdiction: Croatia
Funding stream: ZP
ProjectNumber: 262067
Title (english): Proteomics Research Infrastructure Maximising knowledge EXchange and access (XS)
Acronym: PRIME-XS
Jurisdiction: eu
Funding stream: FP7
Document URLhttp://www.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000495
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) icon
Created on2018-11-07 09:36:29