The role of an amphiphilic helix and transmembrane region in the efficient acylation of the M2 protein from influenza virus.

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 compa

SUBMITTER: Meng X 

PROVIDER: S-EPMC10622425 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature