Biology:Coilin
 Generic protein structure example |
Coilin is a protein that in humans is encoded by the COIL gene.[1][2] Coilin got its name from the coiled shape of the Cajal bodies in which it is found. It was first identified using human autoimmune serum.
Function
Coilin protein is one of the main molecular components of Cajal bodies. Cajal bodies are non-membrane bound nuclear bodies of varying number and composition that are involved in the post-transcriptional modification of small nuclear and small nucleolar RNAs. In addition to its structural role, coilin acts as glue to connect the CB to the nucleolus. The N-terminus of the coilin protein directs its self-oligomerization while the C-terminus influences the number of nuclear bodies assembled per cell. Differential methylation and phosphorylation of coilin likely influences its localization among nuclear bodies and the composition and assembly of Cajal bodies. This gene has pseudogenes on chromosome 4 and chromosome 14.[2]
To study CBs, coilin can be combined with GFP (Green Fluorescent Protein) to form Coilin-GFP hybrid protein. The hybrid protein can then be used to locate CBs underneath a microscope, usually near the nucleolus of the cell. Other proteins that make up the CB include snRNPs and nucleolar snoRNPs.
Coilin has been shown to interact with ataxin 1,[3][4] nucleolar phosphoprotein p130,[5] SMN,[6][7] and SNRPB.[7]
References
- ↑ "Structure, expression and chromosomal localization of human p80-coilin gene". Nucleic Acids Res 22 (21): 4462–9. Dec 1994. doi:10.1093/nar/22.21.4462. PMID 7971277.
- ↑ 2.0 2.1 "Entrez Gene: COIL coilin". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8161.
- ↑ "p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product". Biochim. Biophys. Acta 1638 (1): 35–42. May 2003. doi:10.1016/s0925-4439(03)00038-3. PMID 12757932.
- ↑ "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1". Biochem. Biophys. Res. Commun. 371 (2): 256–60. Jun 2008. doi:10.1016/j.bbrc.2008.04.066. PMID 18439907.
- ↑ "Nopp140 functions as a molecular link between the nucleolus and the coiled bodies". J. Cell Biol. 142 (2): 319–29. Jul 1998. doi:10.1083/jcb.142.2.319. PMID 9679133.
- ↑ "Coilin methylation regulates nuclear body formation". Dev. Cell 3 (3): 329–37. Sep 2002. doi:10.1016/s1534-5807(02)00222-8. PMID 12361597.
- ↑ 7.0 7.1 "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein". Genes Dev. 15 (20): 2720–9. Oct 2001. doi:10.1101/gad.908401. PMID 11641277.
Further reading
- "Cajal bodies and coilin — moving towards function". J. Cell Biol. 159 (1): 17–21. October 14, 2002. doi:10.1083/jcb.200206111. PMID 12379800.
- "Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin". J. Exp. Med. 173 (6): 1407–19. 1991. doi:10.1084/jem.173.6.1407. PMID 2033369.
- "Mutational analysis of p80 coilin indicates a functional interaction between coiled bodies and the nucleolus". J. Cell Biol. 131 (4): 817–31. 1996. doi:10.1083/jcb.131.4.817. PMID 7490287.
- "Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis--evidence that the coiled body is a kinetic nuclear structure". J. Cell Biol. 120 (4): 841–52. 1993. doi:10.1083/jcb.120.4.841. PMID 7679389.
- "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics 23 (1): 42–50. 1995. doi:10.1006/geno.1994.1457. PMID 7829101.
- "Assignment of a human autoimmune antigen, p80-coilin gene to chromosome 17q21-q23 and of its possible pseudogene to chromosome 14". Hum. Genet. 95 (2): 233–4. 1995. doi:10.1007/BF00209411. PMID 7860074.
- "Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus". Exp. Cell Res. 230 (1): 84–93. 1997. doi:10.1006/excr.1996.3380. PMID 9013710.
- "Dynamics of distribution of splicing components relative to the transcriptional state of human oocytes from antral follicles". J. Cell. Biochem. 69 (1): 72–80. 1998. doi:10.1002/(SICI)1097-4644(19980401)69:1<72::AID-JCB8>3.0.CO;2-S. PMID 9513048.
- "[Splicing factors in oocyte nuclei from human antral follicles]". Tsitologiia 40 (4): 239–47. 1998. PMID 9644758.
- "Nopp140 functions as a molecular link between the nucleolus and the coiled bodies". J. Cell Biol. 142 (2): 319–29. 1998. doi:10.1083/jcb.142.2.319. PMID 9679133.
- "Cell cycle-dependent localization of the CDK2-cyclin E complex in Cajal (coiled) bodies". J. Cell Sci. 113 (9): 1543–52. 2000. doi:10.1242/jcs.113.9.1543. PMID 10751146.
- "Self-association of coilin reveals a common theme in nuclear body localization". Mol. Biol. Cell 11 (12): 4159–71. 2001. doi:10.1091/mbc.11.12.4159. PMID 11102515.
- "Nuclear gems and Cajal (coiled) bodies in fetal tissues: nucleolar distribution of the spinal muscular atrophy protein, SMN". Exp. Cell Res. 265 (2): 252–61. 2001. doi:10.1006/excr.2001.5186. PMID 11302690.
- "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein". Genes Dev. 15 (20): 2720–9. 2001. doi:10.1101/gad.908401. PMID 11641277.
- "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN". J. Cell Sci. 114 (Pt 24): 4407–19. 2002. doi:10.1242/jcs.114.24.4407. PMID 11792806. https://jcs.biologists.org/content/114/24/4407.
- "Coilin methylation regulates nuclear body formation". Dev. Cell 3 (3): 329–37. 2002. doi:10.1016/S1534-5807(02)00222-8. PMID 12361597.
- "Control of Cajal body number is mediated by the coilin C-terminus". J. Cell Sci. 116 (Pt 2): 303–12. 2003. doi:10.1242/jcs.00211. PMID 12482916.
- "Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivo". J. Cell Sci. 116 (Pt 10): 2039–50. 2004. doi:10.1242/jcs.00400. PMID 12679382.
- "Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines". J. Cell Sci. 122 (Pt 11): 1872–81. 2009. doi:10.1242/jcs.044040. PMID 19435804.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
 |  |
