title: Hsp90-binding immunophilins in plants: the protein movers.
abstract: 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.
authors.affiliation: Dept Pharmacology, University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: W B
authors.initials: WB
authors.lastname: Pratt
authors.forename: P
authors.initials: P
authors.lastname: Krishna
authors.forename: L J
authors.initials: LJ
authors.lastname: Olsen
mesh_terms: D000818:Animals; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D020104:Immunophilins / Q000378:metabolism*; D020675:Peroxisomes / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants; D011485:Protein Binding; D021381:Protein Transport; D011965:Receptors, Glucocorticoid / Q000378:metabolism; D020449:Repetitive Sequences, Amino Acid
chemical_list: D018841:HSP90 Heat-Shock Proteins; D010940:Plant Proteins; D011965:Receptors, Glucocorticoid; D020104:Immunophilins