Hsp90-binding immunophilins in plants: the protein movers

Trends Plant Sci. 2001 Feb;6(2):54-8. doi: 10.1016/s1360-1385(00)01843-4.


Studies of cytoplasmic-nuclear trafficking of the glucocorticoid receptor in mammalian cells suggest that the hsp90/hsp70-based chaperone system and the hsp90-binding immunophilin FKBP52 are involved in targeted movement of the receptor along microtubule tracts. Over the past few years, plant cells have been found to possess a similar multiprotein chaperone machinery. Plant cells also contain high molecular weight FKBPs that bind to plant hsp90 via a conserved protein interaction involving tetratricopeptide repeat domains. The hsp90/hsp70-based machinery and the plant FKBPs might be used to target the trafficking of signalling proteins in plants.

Publication types

  • Review

MeSH terms

  • Animals
  • HSP90 Heat-Shock Proteins / metabolism*
  • Immunophilins / metabolism*
  • Peroxisomes / metabolism
  • Plant Proteins / metabolism*
  • Plants
  • Protein Binding
  • Protein Transport
  • Receptors, Glucocorticoid / metabolism
  • Repetitive Sequences, Amino Acid


  • HSP90 Heat-Shock Proteins
  • Plant Proteins
  • Receptors, Glucocorticoid
  • Immunophilins