FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa.
FKBP22 is a dimeric protein in the lumen of the endoplasmic reticulum, which exhibits a chaperone as well as a PPIase activity. It binds via its FK506 binding protein (FKBP) domain directly to the Hsp70 chaperone BiP that stimulates the chaperone activity of FKBP22. Here we demonstrate additionally the association of FKBP22 with the molecular chaperones and folding catalysts Grp170, alpha-subunit of glucosidase II, PDI, ERp38, and CyP23. These proteins are associated with FKBP22 in at least two protein complexes. Furthermore, we report an essential role for FKBP22 in the development of microconidiophores in Neurospora crassa.
Tremmel
Dirk
D
Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und molekulare Zellforschung, Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.
Duarte
Margarida
M
Videira
Arnaldo
A
Tropschug
Maximilian
M
D002384:Catalysis; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000032:analysis / Q000737:chemistry; D017353:Gene Deletion; D013058:Mass Spectrometry; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D009492:Neurospora crassa / Q000166:cytology / Q000378:metabolism* / Q000502:physiology; D011485:Protein Binding; D017510:Protein Folding; D013172:Spores, Fungal / Q000378:metabolism; D022021:Tacrolimus Binding Proteins / Q000737:chemistry* / Q000378:metabolism*
D005656:Fungal Proteins; D018832:Molecular Chaperones; C403422:FKBP22; D022021:Tacrolimus Binding Proteins