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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease.

Focal adhesion plaques were severely affected in human embryonic fibroblasts permeabilized with digitonin and incubated in buffer containing the human immunodeficiency virus type 1 protease (HIV-1 PR). A mutant HIV-1 PR (3271 HIV-1 PR) had no effect on focal adhesion plaques. Similar effects were seen with cells microinjected with either HIV-1 PR or 3271 HIV-1 PR. Immunoblots of the human embryonic fibroblasts demonstrated that a number of focal adhesion plaque proteins were specifically cleaved by HIV-1 PR. These included fimbrin, focal adhesion plaque kinase ( FAK), talin, and, to a lesser extent, filamin, spectrin and fibronectin. Proteins detected by antibodies to beta 4 integrin and alpha 3 integrin were also cleaved by the HIV-1 PR. Control experiments demonstrated that the effect and protein cleavages described are due to action of the HIV-1 PR and not to the action of endogenous host cell proteases.[1]


  1. Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. Shoeman, R.L., Hartig, R., Hauses, C., Traub, P. Cell Biol. Int. (2002) [Pubmed]
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