[HTML][HTML] Protein disulfide isomerase directly interacts with β-actin Cys374 and regulates cytoskeleton reorganization
K Sobierajska, S Skurzynski, M Stasiak… - Journal of Biological …, 2014 - ASBMB
Recent studies support the role of cysteine oxidation in actin cytoskeleton reorganization
during cell adhesion. The aim of this study was to explain whether protein disulfide
isomerase (PDI) is responsible for the thiol-disulfide rearrangement in the β-actin molecule
of adhering cells. First, we showed that PDI forms a disulfide-bonded complex with β-actin
with a molecular mass of 110 kDa. Specific interaction of both proteins was demonstrated by
a solid phase binding assay, surface plasmon resonance analysis, and immunoprecipitation …
during cell adhesion. The aim of this study was to explain whether protein disulfide
isomerase (PDI) is responsible for the thiol-disulfide rearrangement in the β-actin molecule
of adhering cells. First, we showed that PDI forms a disulfide-bonded complex with β-actin
with a molecular mass of 110 kDa. Specific interaction of both proteins was demonstrated by
a solid phase binding assay, surface plasmon resonance analysis, and immunoprecipitation …