biostudies-literatureVlach JNCI NIH HHS10565-70https://www.ebi.ac.uk/biostudies/studies/S-EPMC2492450biostudies-literatureUnknown105(30)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 buProceedings of the National Academy of Sciences of the United States of AmericaD-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.PMC2492450R01 CA027834R37 CA027834Lipov JHunter EVlach JLang JVeverka VSrb PPichova IRuml THrabal RRumlova MKnejzlik ZfalseD-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.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 bu2008-01-01T00:00:00Z2008 Jul2026-05-02T06:23:53.813Z2026-04-07T17:41:18.001ZS-EPMC24924501864783910.1073/pnas.0801765105