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Interdomain flexibility in the plakin domain, analysis by small angle x-ray scattering

AuthorsManso, José A. ; Carballido Vázquez, Ana M. ; Pereda, José M. de
Issue Date2014
CitationSBE 2014
AbstractPlakins are a family of large proteins that cross-link filament systems of the cytoskeleton and tether them to membrane associated structures. Plakins are essential for the integrity of tissues exposed to mechanical stress such as the skin and muscle, and they are also important in the nervous system. Mammalian plakins include plectin, desmoplakin, the bullous pemphigoid antigen 1 (BPAG1), the microtubule actin crosslinking factor 1, envoplakin, periplakin, and epiplakin. Plakins are high molecular weight proteins with a modular structure divided in three distinct regions, the N- and C-terminal regions harbor binding sites for other proteins and are separated by a central rod domain. The N-terminal segment contains a region conserved in most plakins, named the plakin domain, which is responsible for the subcellular localization of these proteins. Plectin contains a complete plakin domain formed by an array of nine spectrin repeats (SR1-SR9) and an SH3 domain inserted in the SR5. Each SR is a three helix bundle; adjacent SRs are connected by helical linkers and form elongated structures. Nonetheless, the SR2 and SR3 are connected by a non-helical linker. Upstream the SR1, plectin contains an actin binding domain (ABD) formed by two calponin-homology domains. The ABD and the SR1 are connected by a short non-helical linker. On the other hand, the epithelial variant of BPAG1 (BPAG1e) lacks the ABD and the SR1. Here, we have used small angle x-ray scattering to analyze the interdomain conformational variability in the N-terminal region of the plakin domains of plectin and BPAG1e. The scattering data were analyzed using the ensemble optimization method. Our results suggest that the N-terminal region of plakins resemble articulated structures formed by apparently rigid segments connected by flexible hinges.
DescriptionResumen del trabajo presentado al XIVth Congress of the Spanish Biophysical Society, celebrado en Alcalá de Henares (Madrid-España) del 11 al 13 de junio de 2014.
Appears in Collections:(IBMCC) Comunicaciones congresos
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