Please use this identifier to cite or link to this item:
Title: D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.
Authors: Vlach, J
Lipov, J
Rumlová, M
Veverka, V
Lang, J
Srb, P
Knejzlík, Z
Pichová, I
Hunter, E
Hrabal, R
Ruml, T
First Published: 29-Jul-2008
Citation: PROC NATL ACAD SCI U S A, 2008, 105 (30), pp. 10565-10570
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 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.
DOI Link: 10.1073/pnas.0801765105
eISSN: 1091-6490
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.