Phosphorylation of the HTLV-1 matrix L-domain-containing protein by virus-associated ERK-2 kinase

Virology
Bénédicte HemonnotLaurence Briant

Abstract

L-domain-containing proteins from animal retroviruses play a critical role in the recruitment of the host cell endocytic machinery that is required for retroviruses budding. We recently demonstrated that phosphorylation of the p6(gag) protein containing the L-domain of the human immunodeficiency virus type 1 regulates viral assembly and budding. Here, we investigated whether or not the L-domain-containing protein from another human retrovirus, namely the matrix protein of the human T-cell leukemia virus type 1, that contains the canonical PTAP and PPPY L-domain motifs, shares similar functional properties. We found that MA is phosphorylated at several sites. We identified one phosphorylated amino acid in the HTLV-1 MA protein as being S105, located in the close vicinity to the L-domain sequence. S105 phosphorylation was found to be mediated by the cellular kinase ERK-2 that is incorporated within HTLV-1 virus particles in an active form. Mutation of the ERK-2 target S105 residue into an alanine was found to decrease viral release and budding efficiency of the HTLV-1(ACH) molecular clone from transfected cells. Our data thus support the postulate that phosphorylation of retroviral L-domain proteins is a common feature to retrovi...Continue Reading

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Citations

Sep 6, 2011·Retrovirology·Charline GiroudLaurence Briant
Oct 14, 2011·Viruses·Michael D LairmorePatrick L Green
Feb 18, 2010·Biochimie·Imen Najjar, Remi Fagard
Jul 6, 2016·Frontiers in Microbiology·Ayumi KudohAkihide Ryo
Jan 25, 2007·Molecular Therapy : the Journal of the American Society of Gene Therapy·Iana HaralambievaKah-Whye Peng
Nov 1, 2016·Journal of Virology·Jonathon D BrzezinskiMonica J Roth
Apr 4, 2021·International Journal of Molecular Sciences·Charlotte BussienneSerena Bernacchi

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