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Activation of p21-Activated Kinase 2 by Human Immunodeficiency Virus Type 1 Nef Induces Merlin Phosphorylation

Bangdong L. Wei,¹ Vivek K. Arora,^1, Alexa Raney,¹ Lillian S. Kuo,¹ Guang-Hui Xiao,² Eduardo O'Neill,¹ Joseph R. Testa,² John L. Foster,¹ and J. Victor Garcia^1*

Department of Internal Medicine, Division of Infectious Diseases, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390,¹ Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111²

Received 28 July 2005/ Accepted 12 September 2005

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.

Present address: Massachusetts General Hospital, Department of Medicine, 55 Fruit Street, Boston, MA 02114.

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