[HTML][HTML] Oxidation and nitrosylation of cysteines proximal to the intermediate filament (IF)-binding site of plectin: effects on structure and vimentin binding and …
R Spurny, K Abdoulrahman, L Janda… - Journal of biological …, 2007 - ASBMB
As an intermediate filament (IF)-based cytolinker protein, plectin plays a key role in the
maintenance of cellular cytoarchitecture and serves at the same time as a scaffolding
platform for signaling cascades. Consisting of six structural repeats (R1–6) and harboring
binding sites for different IF proteins and proteins involved in signaling, the plectin C-
terminal domain is of strategic functional importance. Depending on the species, it contains
at least 13 cysteines, 4 of which reside in the R5 domain. To investigate the structural and …
maintenance of cellular cytoarchitecture and serves at the same time as a scaffolding
platform for signaling cascades. Consisting of six structural repeats (R1–6) and harboring
binding sites for different IF proteins and proteins involved in signaling, the plectin C-
terminal domain is of strategic functional importance. Depending on the species, it contains
at least 13 cysteines, 4 of which reside in the R5 domain. To investigate the structural and …