Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell Biol Int. 2002;26(6):529-39.

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

Author information

  • 1Max-Planck-Institut für Zellbiologie, Rosenhof, 68526 Ladenburg, Germany. rshoeman@zellbio.mpg.de

Abstract

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.

PMID:
12119179
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Portland Press
    Loading ...
    Write to the Help Desk