Hinged plakin domains provide specialized degrees of articulation in envoplakin, periplakin and desmoplakin

Caezar Al-Jassar, Pau Bernadό, Martyn Chidgey, Michael Overduin

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)
155 Downloads (Pure)

Abstract

Envoplakin, periplakin and desmoplakin are cytoskeletal proteins that provide structural integrity within the skin and heart by resisting shear forces. Here we reveal the nature of unique hinges within their plakin domains that provides divergent degrees of flexibility between rigid long and short arms composed of spectrin repeats. The range of mobility of the two arms about the hinge is revealed by applying the ensemble optimization method to small-angle X-ray scattering data. Envoplakin and periplakin adopt 'L' shaped conformations exhibiting a 'helicopter propeller'-like mobility about the hinge. By contrast desmoplakin exhibits essentially unrestricted mobility by 'jack-knifing' about the hinge. Thus the diversity of molecular jointing that can occur about plakin hinges includes 'L' shaped bends, 'U' turns and fully extended 'I' orientations between rigid blocks of spectrin repeats. This establishes specialised hinges in plakin domains as a key source of flexibility that may allow sweeping of cellular spaces during assembly of cellular structures and could impart adaptability, so preventing irreversible damage to desmosomes and the cell cytoskeleton upon exposure to mechanical stress.
Original languageEnglish
Article numbere69767
JournalPLoS ONE
Volume8
Issue number7
DOIs
Publication statusPublished - 29 Jul 2013

Keywords

  • Crystal structure
  • Cytoskeletal proteins
  • Desmosomes
  • Protein structure
  • Sequence alignment
  • Small-angle scattering
  • Spectrins
  • Structural proteins

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