Publication Abstract from PubMed
Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms.
D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.,Vlach J, Lipov J, Rumlova M, Veverka V, Lang J, Srb P, Knejzlik Z, Pichova I, Hunter E, Hrabal R, Ruml T Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10565-70. Epub 2008 Jul 22. PMID:18647839[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
