Activation of p21-activated kinase 2 by human immunodeficiency virus type 1 Nef induces merlin phosphorylation

Bangdong L. Wei, Vivek K. Arora, Alexa Raney, Lillian S. Kuo, Guang Hui Xiao, Eduardo O'Neill, Joseph R. Testa, John L. Foster, J. Victor Garcia

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The accessory human immunodeficiency virus type 1 (HIV-1) protein Nef activates the autophosphorylation activity of p21-activated kinase 2 (PAK2). Merlin, a cellular substrate of PAK2, is homologous to the ezrin-radixin-moesin family and plays a critical role in Rac signaling. To assess the possible impact on host cell metabolism of Nef-induced PAK2 activation, we investigated the phosphorylation of merlin in Nef expressing cells. Here we report that Nef induces merlin phosphorylation in multiple cell lines independently of protein kinase A. This intracellular phosphorylation of merlin directly correlates with in vitro assay of the autophosphorylation activity of Nef-activated PAK2. Importantly, merlin phosphorylation induced by Nef was also observed in human primary T cells. The finding that Nef induces phosphorylation of the key signaling molecule merlin suggests several possible roles for PAK2 activation in HIV pathogenesis.

Original languageEnglish
Pages (from-to)14976-14980
Number of pages5
JournalJournal of virology
Volume79
Issue number23
DOIs
StatePublished - Dec 2005

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