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Structure of the plakin domain of plectin: implications for the mechanical properties of plakins

AutorOrtega, Esther ; Manso, José A. ; Buey, Ruben M.; Carballido Vázquez, Ana M. ; Carabias, Arturo ; Sonnenberg, Arnoud; Pereda, José M. de
Fecha de publicación2016
CitaciónCNIC Conference: Mechanical forces in physiology and disease (2016)
ResumenPlakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. For example in epithelia plectin links the cytokeratins to the integrin α6ß4 in the hemidesmosomes. The N-terminal region of plectin contains an actin binding domain that mediates the binding to α6ß4, and a region named the plakin domain that is conserved in most plakins. The plakin domain of plectin is formed by nine spectrin repeats (SR1 to SR9) and a non-canonical SH3 domain. We have combined X-ray crystallography with small angle X-ray scattering (SAXS) to elucidate the global structure of the plakin domain of plectin, extending our previous analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 segment allowed us to characterize its uniquely wide inter-repeat conformational variability. We also report the crystal structures of the SR7-SR8 region, refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region, which is conserved in all other plakin domains, forms a rigid segment stabilized by uniquely extensive inter-repeat contacts mediated by unusually long helices in SR8 and SR9. Using SAXS we show that in solution the SR3-SR9 of plectin has an extended shape with a small central kink. Other plakins, such as bullous pemphigoid antigen 1 (BPAG1) and microtubule and actin crosslinking factor 1 (MACF1), are likely to have similar extended plakin domains. The array of SRs in the plakin domain is very similar to those present in spectrins. Such arrays of SRs form deformable structures that can be bent; SRs can also unfold individually at low pulling forces. The continuous and extended rod-like structure of plectin suggests that the plakin domain may work as a molecular shock absorbent that dissipates elastic energy when cells are subjected to external forces, and might contribute to the mechanical stability and resilience of tissues that are subjected to mechanical stress
DescripciónResumen del póster presentado a la CNIC Conference: Mechanical forces in physiology and disease, celebrada en Madrid (España) del 4 al 5 de noviembre de 2016.
URIhttp://hdl.handle.net/10261/169563
Aparece en las colecciones: (IBMCC) Comunicaciones congresos
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