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Poliovirus infection results in resistance of infected cells to apoptotic stimuli. Viral proteins involved in such functions usually target key cellular regulators. Here we demonstrate that viral protein 3A binds and inactivates LIS1, a component of the dynein/dynactin motor complex, encoded by the gene mutated in patients with type I lissencephaly („smooth brain‰), thus causing rapid disappearence of TNF and interferon receptors from the plasma membrane. Like 3A, truncated derivatives of LIS, acting in a dominant negative manner, deregulate endoplasmatic reticilum -to-Golgi vesicular transport and eliminate unstable receptors from the cell surface. Protein 3A locks Golgi-targeted YFP in endoplasmatic reticilum, while expression of LIS1 mutants results in a dispersed cytoplasmic localization of the reporter protein. LIS1 dysfunction caused by ectopic expressing 3A or LIS1 mutants, as well as by overexpression of wild …