Biology:FKBP1B
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.[1][2]
Function
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin (sirolimus). It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.[2]
Clinical significance
Defective interaction between FKB1B and the ryanodine receptor is thought to be a potential mechanism underlying the arrhythmias seen in those with the genetic condition catecholaminergic polymorphic ventricular tachycardia.[3]
References
- ↑ "Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts". Biochemical and Biophysical Research Communications 200 (2): 836–43. April 1994. doi:10.1006/bbrc.1994.1527. PMID 7513996.
- ↑ 2.0 2.1 "Entrez Gene: FKBP1B FK506 binding protein 1B, 12.6 kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2281.
- ↑ Venetucci, Luigi; Denegri, Marco; Napolitano, Carlo; Priori, Silvia G. (October 2012). "Inherited calcium channelopathies in the pathophysiology of arrhythmias". Nature Reviews. Cardiology 9 (10): 561–575. doi:10.1038/nrcardio.2012.93. ISSN 1759-5010. PMID 22733215.
Further reading
- "Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters 495 (1–2): 1–6. April 2001. doi:10.1016/S0014-5793(01)02326-2. PMID 11322937.
- "A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor". The Journal of Biological Chemistry 270 (44): 26511–22. November 1995. doi:10.1074/jbc.270.44.26511. PMID 7592869.
- "Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes". The Journal of Biological Chemistry 272 (6): 3133–6. February 1997. doi:10.1074/jbc.272.6.3133. PMID 9013543.
- "Structure of FKBP12.6 in complex with rapamycin". Acta Crystallographica D 56 (Pt 3): 266–71. March 2000. doi:10.1107/S0907444999016571. PMID 10713512.
- "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts". Cell 101 (4): 365–76. May 2000. doi:10.1016/S0092-8674(00)80847-8. PMID 10830164.
- "FKBP binding characteristics of cardiac microsomes from diverse vertebrates". Biochemical and Biophysical Research Communications 281 (4): 979–86. March 2001. doi:10.1006/bbrc.2001.4444. PMID 11237759.
- "In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6". The Biochemical Journal 370 (Pt 2): 579–89. March 2003. doi:10.1042/BJ20021433. PMID 12443530.
- "Localization of the 12.6-kDa FK506-binding protein (FKBP12.6) binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (ryanodine receptor)". The Journal of Biological Chemistry 278 (6): 3786–92. February 2003. doi:10.1074/jbc.M210962200. PMID 12446682.
- "The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations". Biochemical and Biophysical Research Communications 299 (4): 594–8. December 2002. doi:10.1016/S0006-291X(02)02689-X. PMID 12459180.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–903. December 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6". The Journal of Biological Chemistry 278 (31): 28856–64. August 2003. doi:10.1074/jbc.M212440200. PMID 12754204.
- "Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor". Biochemical and Biophysical Research Communications 323 (1): 91–7. October 2004. doi:10.1016/j.bbrc.2004.08.060. PMID 15351706.
- "Evidence of association between FKBP1B and thyroid autoimmune disorders in a large Tunisian family". Autoimmunity 37 (3): 237–9. May 2004. doi:10.1080/08916930410001702478. PMID 15497458.
- "Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain". The Journal of Biological Chemistry 280 (7): 5475–85. February 2005. doi:10.1074/jbc.M412954200. PMID 15591045.
- "A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia". International Journal of Cardiology 99 (2): 343–5. March 2005. doi:10.1016/j.ijcard.2003.11.050. PMID 15749201.
- "Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure". Proceedings of the National Academy of Sciences of the United States of America 102 (27): 9607–12. July 2005. doi:10.1073/pnas.0500353102. PMID 15972811. Bibcode: 2005PNAS..102.9607W.
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