Plectin: a cytolinker by design

Biol Chem. 1999 Feb;380(2):151-8. doi: 10.1515/BC.1999.023.


Plectin is a cytoskeletal protein of >500 kDa that forms dumbbell-shaped homodimers comprising a central parallel alpha-helical coiled coil rod domain flanked by globular domains, thus providing a molecular backbone ideally suited to mediate the protein's interactions with an array of other cytoskeletal elements. Plectin self-associates and interacts with actin and intermediate filament cytoskeleton networks at opposite ends, and it binds at both ends to the hemidesmosomal transmembrane protein integrin beta-4, and likely to other junctional proteins. The central coiled coil rod domain can form bridges over long stretches and serves as a flexible linker between the structurally diverse N-terminal domain and the highly conserved C-terminal domain. Plectin is also a target of p34cdc2 kinase that regulates its dissociation from intermediate filaments during mitosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actins / metabolism
  • Animals
  • Antigens, CD / metabolism
  • Cell Cycle
  • Humans
  • Integrin beta4
  • Intermediate Filament Proteins / chemistry
  • Intermediate Filament Proteins / metabolism*
  • Intermediate Filaments / metabolism
  • Plectin
  • Protein Conformation


  • Actins
  • Antigens, CD
  • Integrin beta4
  • Intermediate Filament Proteins
  • PLEC protein, human
  • Plectin