Title |
The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions
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Published in |
Retrovirology, January 2014
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DOI | 10.1186/1742-4690-11-9 |
Pubmed ID | |
Authors |
Ayumi Kudoh, Shoukichi Takahama, Tatsuya Sawasaki, Hirotaka Ode, Masaru Yokoyama, Akiko Okayama, Akiyo Ishikawa, Kei Miyakawa, Satoko Matsunaga, Hirokazu Kimura, Wataru Sugiura, Hironori Sato, Hisashi Hirano, Shigeo Ohno, Naoki Yamamoto, Akihide Ryo |
Abstract |
Human immunodeficiency virus type 1 (HIV-1) Gag is the main structural protein that mediates the assembly and release of virus-like particles (VLPs) from an infected cell membrane. The Gag C-terminal p6 domain contains short sequence motifs that facilitate virus release from the plasma membrane and mediate incorporation of the viral Vpr protein. Gag p6 has also been found to be phosphorylated during HIV-1 infection and this event may affect virus replication. However, the kinase that directs the phosphorylation of Gag p6 toward virus replication remains to be identified. In our present study, we identified this kinase using a proteomic approach and further delineate its role in HIV-1 replication. |
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Mendeley readers
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Computer Science | 3 | 7% |
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