dc.contributor.author
Meng, Xiaorong
dc.contributor.author
Templeton, Clark
dc.contributor.author
Clementi, Cecilia
dc.contributor.author
Veit, Michael
dc.date.accessioned
2023-11-06T06:23:58Z
dc.date.available
2023-11-06T06:23:58Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/41423
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-41145
dc.description.abstract
Protein palmitoylation, a cellular process occurring at the membrane-cytosol interface, is orchestrated by members of the DHHC enzyme family and plays a pivotal role in regulating various cellular functions. The M2 protein of the influenza virus, which is acylated at a membrane-near amphiphilic helix serves as a model for studying the intricate signals governing acylation and its interaction with the cognate enzyme, DHHC20. We investigate it here using both experimental and computational assays. We report that altering the biophysical properties of the amphiphilic helix, particularly by shortening or disrupting it, results in a substantial reduction in M2 palmitoylation, but does not entirely abolish the process. Intriguingly, DHHC20 exhibits an augmented affinity for some M2 mutants compared to the wildtype M2. Molecular dynamics simulations unveil interactions between amino acids of the helix and the catalytically significant DHHC and TTXE motifs of DHHC20. Our findings suggest that the binding of M2 to DHHC20, while not highly specific, is mediated by requisite contacts, possibly instigating the transfer of fatty acids. A comprehensive comprehension of protein palmitoylation mechanisms is imperative for the development of DHHC-specific inhibitors, holding promise for the treatment of diverse human diseases.
en
dc.format.extent
17 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
Biochemistry
en
dc.subject
Computational biophysics
en
dc.subject
Influenza virus
en
dc.subject
Post-translational modifications
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
The role of an amphiphilic helix and transmembrane region in the efficient acylation of the M2 protein from influenza virus
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
18928
dcterms.bibliographicCitation.doi
10.1038/s41598-023-45945-z
dcterms.bibliographicCitation.journaltitle
Scientific Reports
dcterms.bibliographicCitation.volume
13
dcterms.bibliographicCitation.url
https://doi.org/10.1038/s41598-023-45945-z
refubium.affiliation
Veterinärmedizin
refubium.affiliation
Physik
refubium.affiliation.other
Institut für Virologie
![This authority value has been confirmed as accurate by an interactive user](/cache_202e45ad85b55efaeb29160f63cd3f3b/themes/FuCD/images/authority_control/invisible.gif)
refubium.funding
Springer Nature DEAL
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin gefördert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2045-2322