FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa
| Autor: | Margarida Duarte, Dirk Tremmel, Maximilian Tropschug, Arnaldo Videira |
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| Rok vydání: | 2007 |
| Předmět: |
Protein Folding
BiP Biophysics Chaperone Biology Endoplasmic Reticulum Biochemistry Catalysis Mass Spectrometry Fungal Proteins Tacrolimus Binding Proteins Structural Biology Genetics Protein disulfide-isomerase Molecular Biology Neurospora crassa Endoplasmic reticulum Disulfide isomerase Cell Biology Spores Fungal FKBP Prefoldin CDC37 Chaperone (protein) Hsp33 Unfolded protein response biology.protein PPIase Gene Deletion Molecular Chaperones Protein Binding |
| Zdroj: | FEBS letters. 581(10) |
| ISSN: | 0014-5793 |
| Popis: | 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, α-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. |
| Databáze: | OpenAIRE |
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