Disease relevance of Fkbp10

• A null mutation of the Fkbp6 gene causes azoospermia in mice as well as in rats [1].
• Fractionation of differentiating murine teratocarcinoma F9 cells and extraction of the nuclear/microsomal pellets with ethidium bromide led to the purification and microsequencing of the protein mCyP-S1, a novel cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase (PPIase). mCyP-S1 is a new member of the cyclophilin class of proteins [2].

High impact information on Fkbp10

• In the synapsis-defective Fkbp6(-/-) mouse, TopBP1 heavily stains unsynapsed regions of chromosomes [3].
• A polyclonal antibody, raised against a COOH-terminal peptide (amino acid residues 566-581), was used to immunoprecipitate FKBP65 from NIH3T3 cells and demonstrate that FKBP65 is a glycoprotein [4].
• In addition, [32P]orthophosphate labeling experiments show that FKBP65 is also a phosphoprotein [4].
• Based on Northern blot analysis, FKBP65 mRNA transcripts are present in lung, spleen, heart, brain, and testis [4].
• Molecular cloning, DNA sequence analysis, and biochemical characterization of a novel 65-kDa FK506-binding protein (FKBP65) [4].

Biological context of Fkbp10

• Mouse Fkbp10 contains 10 exons and 9 introns encompassing 8.5 kb [5].
• Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family [5].
• We have isolated a unique gene from a mouse JB6 epidermal cell cDNA expression library, termed FKBPRP, that codes for a protein having domains that share between 37 and 44% amino acid sequence identity and 60% similarity with members of the family of FK506-binding proteins [6].
• Unlike any other FKBP characterized so far, FKBP65 is developmentally regulated and may be intimately involved in organogenesis [5].
• We have isolated a gene from a cDNA library generated from the thymus of a mouse with severe combined immune deficiency, termed FKBP9, that encodes a protein related to FK506-binding protein 6 (65 kDa, FKBP65) [7].

Anatomical context of Fkbp10

• Recently, the targeted inactivation of Fkbp6 in mice has been observed to result in aspermic males and the absence of normal pachytene spermatocytes [8].

Associations of Fkbp10 with chemical compounds

• It belongs to a growing family including other FKBPs which bind the immunosuppressants FK506 and rapamycin, and cyclophilins which bind cyclosporin A, all having rotamase (peptidyl-prolyl cis-trans isomerase) activity which may be involved in protein folding [9].

References