{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vlach J"],"funding":["NCI NIH HHS"],"pagination":["10565-70"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2492450"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["105(30)"],"pubmed_abstract":["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 bu"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein."],"pmcid":["PMC2492450"],"funding_grant_id":["R01 CA027834","R37 CA027834"],"pubmed_authors":["Lipov J","Hunter E","Vlach J","Lang J","Veverka V","Srb P","Pichova I","Ruml T","Hrabal R","Rumlova M","Knejzlik Z"],"additional_accession":[]},"is_claimable":false,"name":"D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.","description":"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 bu","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Jul","modification":"2026-05-02T06:23:53.813Z","creation":"2026-04-07T17:41:18.001Z"},"accession":"S-EPMC2492450","cross_references":{"pubmed":["18647839"],"doi":["10.1073/pnas.0801765105"]}}