Coilin and Cajal bodies

References

• Gall JG. Cajal bodies: The first 100 years. Annu Rev Cell Dev Biol. 2000;16(1):273–10. doi: 10.1146/annurev.cellbio.16.1.273
   PubMedGoogle Scholar
• Cajal SR. Un sencillo metodo de coloracion seletiva del reticulo protoplasmatico y sus efectos en los diversos organos nerviosos de vertebrados e invertebrados. Trab Lab Invest Biol (Madrid). 1903;2:129–221.
   Google Scholar
• Lafarga M, Tapia O, Romero AM, et al. Cajal bodies in neurons. RNA Biol. 2017;14(6):712–725. doi: 10.1080/15476286.2016.1231360
   PubMed Web of Science ®Google Scholar
• Andrade LE, Chan EK, Raska I, et al. Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin. J Exp Med. 1991;173(6):1407–1419. doi: 10.1084/jem.173.6.1407
   PubMed Web of Science ®Google Scholar
• Raska I, Andrade LE, Ochs RL, et al. Immunological and ultrastructural studies of the nuclear coiled body with autoimmune antibodies. Exp Cell Res. 1991;195(1):27–37. doi: 10.1016/0014-4827(91)90496-H
   PubMed Web of Science ®Google Scholar
• Carmo-Fonseca M, Pepperkok R, Sproat BS, et al. In vivo detection of snRNP-rich organelles in the nuclei of mammalian cells. EMBO J. 1991;10(7):1863–1873. doi: 10.1002/j.1460-2075.1991.tb07712.x
   PubMed Web of Science ®Google Scholar
• Carmo-Fonseca M, Tollervey D, Pepperkok R, et al. Mammalian nuclei contain foci which are highly enriched in components of the pre-mRNA splicing machinery. EMBO J. 1991;10(1):195–206. doi: 10.1002/j.1460-2075.1991.tb07936.x
   PubMed Web of Science ®Google Scholar
• Carmo-Fonseca M, Pepperkok R, Carvalho MT, et al. Transcription-dependent colocalization of the U1, U2, U4/U6, and U5 snRNPs in coiled bodies. J Cell Bio. 1992;117(1):1–14. doi: 10.1083/jcb.117.1.1
   PubMed Web of Science ®Google Scholar
• Frey MR, Matera AG. Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells. Proc Natl Acad Sci U S A. 1995;92(13):5915–5919. doi: 10.1073/pnas.92.13.5915
   PubMed Web of Science ®Google Scholar
• Gao L, Frey MR, Matera AG. Human genes encoding U3 snRNA associate with coiled bodies in interphase cells and are clustered on chromosome 17p11.2 in a complex inverted repeat structure. Nucleic Acids Res. 1997;25(23):4740–4747. doi: 10.1093/nar/25.23.4740
   PubMed Web of Science ®Google Scholar
• Smith KP, Carter KC, Johnson CV, et al. U2 and U1 snRNA gene loci associate with coiled bodies. J Cell Biochem. 1995;59(4):473–485. doi: 10.1002/jcb.240590408
   PubMed Web of Science ®Google Scholar
• Schul W, Adelaar B, van Driel R, et al. Coiled bodies are predisposed to a spatial association with genes that contain snoRNA sequences in their introns. J Cell Biochem. 1999;75(3):393–403. doi: 10.1002/(SICI)1097-4644(19991201)75:3<393:AID-JCB5>3.0.CO;2-G
   PubMed Web of Science ®Google Scholar
• Jacobs EY, Frey MR, Wu W, et al. Coiled bodies preferentially associate with U4, U11, and U12 small nuclear RNA genes in interphase HeLa cells but not with U6 and U7 genes. Mol Biol Cell. 1999;10(5):1653–1663. doi: 10.1091/mbc.10.5.1653
   PubMed Web of Science ®Google Scholar
• Machyna M, Kehr S, Straube K, et al. The coilin interactome identifies hundreds of small noncoding RNAs that traffic through Cajal bodies. Mol Cell. 2014;56(3):389–399. doi: 10.1016/j.molcel.2014.10.004
   PubMed Web of Science ®Google Scholar
• Wang Q, Sawyer IA, Sung MH, et al. Cajal bodies are linked to genome conformation. Nat Commun. 2016;7(1):10966. doi: 10.1038/ncomms10966
   PubMedGoogle Scholar
• Frey MR, Bailey AD, Weiner AM, et al. Association of snRNA genes with coiled bodies is mediated by nascent snRNA transcripts. Curr Biol. 1999;9(3):126–135. doi: 10.1016/S0960-9822(99)80066-9
   PubMed Web of Science ®Google Scholar
• Smith KP, Lawrence JB, Gall J. Interactions of U2 gene loci and their nuclear transcripts with Cajal (coiled) bodies: evidence for PreU2 within Cajal bodies. Mol Biol Cell. 2000;11(9):2987–2998. doi: 10.1091/mbc.11.9.2987
   PubMed Web of Science ®Google Scholar
• Suzuki T, Izumi H, Ohno M. Cajal body surveillance of U snRNA export complex assembly. J Cell Bio. 2010;190(4):603–612. doi: 10.1083/jcb.201004109
   PubMed Web of Science ®Google Scholar
• Lardelli RM, Schaffer AE, Eggens VR, et al. Biallelic mutations in the 3´ exonuclease TOE1 cause pontocerebellar hypoplasia and uncover a role in snRNA processing. Nat Genet. 2017;49(3):457–464. doi: 10.1038/ng.3762
   PubMed Web of Science ®Google Scholar
• Son A, Park JE, Kim VN. PARN and TOE1 constitute a 3´ end maturation module for nuclear non-coding RNAs. Cell Rep. 2018;23(3):888–898. doi: 10.1016/j.celrep.2018.03.089
   PubMed Web of Science ®Google Scholar
• Kiss AM, Jady BE, Darzacq X, et al. A Cajal body-specific pseudouridylation guide RNA is composed of two box H/ACA snoRNA-like domains. Nucleic Acids Res. 2002;30(21):4643–4649. doi: 10.1093/nar/gkf592
   PubMed Web of Science ®Google Scholar
• Jady BE, Darzacq X, Tucker KE, et al. Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm. EMBO J. 2003;22(8):1878–1888. doi: 10.1093/emboj/cdg187
   PubMed Web of Science ®Google Scholar
• Duchemin A, O’Grady T, Hanache S, et al. DHX15-independent roles for TFIP11 in U6 snRNA modification, U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing fidelity. Nat Commun. 2021;12(1):6648. doi: 10.1038/s41467-021-26932-2
   PubMed Web of Science ®Google Scholar
• Narayanan A, Speckmann W, Terns R, et al. Role of the box C/D motif in localization of small nucleolar RNAs to coiled bodies and nucleoli. MBoC. 1999;10(7):2131–2147. doi: 10.1091/mbc.10.7.2131
   Google Scholar
• Gall JG, Bellini M, Wu Z, et al. Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes. Mol Biol Cell. 1999;10(12):4385–4402. doi: 10.1091/mbc.10.12.4385
   PubMed Web of Science ®Google Scholar
• Pradet-Balade B, Girard C, Boulon S, et al. CRM1 controls the composition of nucleoplasmic pre-snoRNA complexes to licence them for nucleolar transport. EMBO J. 2011;30(11):2205–2218. doi: 10.1038/emboj.2011.128
   PubMed Web of Science ®Google Scholar
• Verheggen C, Lafontaine DL, Samarsky D, et al. Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments. EMBO J. 2002;21(11):2736–2745. doi: 10.1093/emboj/21.11.2736
   PubMed Web of Science ®Google Scholar
• Boulon S, Verheggen C, Jady BE, et al. PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli. Mol Cell. 2004;16(5):777–787. doi: 10.1016/j.molcel.2004.11.013
   PubMed Web of Science ®Google Scholar
• Massenet S, Bertrand E, Verheggen C. Assembly and trafficking of box C/D and H/ACA snoRNPs. RNA Biol. 2017;14(6):680–692. doi: 10.1080/15476286.2016.1243646
   PubMed Web of Science ®Google Scholar
• Carmo-Fonseca M, Ferreira J, Lamond AI. Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis--evidence that the coiled body is a kinetic nuclear structure. J Cell Bio. 1993;120(4):841–852. doi: 10.1083/jcb.120.4.841
   PubMed Web of Science ®Google Scholar
• Ferreira JA, Carmo-Fonseca M, Lamond AI. Differential interaction of splicing snRNPs with coiled bodies and interchromatin granules during mitosis and assembly of daughter cell nuclei. J Cell Bio. 1994;126(1):11–23. doi: 10.1083/jcb.126.1.11
   PubMed Web of Science ®Google Scholar
• Haaf T, Ward DC. Inhibition of RNA polymerase II transcription causes chromatin decondensation, loss of nucleolar structure, and dispersion of chromosomal domains. Exp Cell Res. 1996;224(1):163–173. doi: 10.1006/excr.1996.0124
   PubMed Web of Science ®Google Scholar
• Pena E, Berciano MT, Fernandez R, et al. Neuronal body size correlates with the number of nucleoli and Cajal bodies, and with the organization of the splicing machinery in rat trigeminal ganglion neurons. J Comp Neurol. 2001;430(2):250–263. doi: 10.1002/1096-9861(20010205)430:2<250:AID-CNE1029>3.0.CO;2-L
   PubMed Web of Science ®Google Scholar
• Tapia O, Narcis JO, Riancho J, et al. Cellular bases of the RNA metabolism dysfunction in motor neurons of a murine model of spinal muscular atrophy: role of Cajal bodies and the nucleolus. Neurobiol Dis. 2017;108:83–99. doi: 10.1016/j.nbd.2017.08.004
   PubMed Web of Science ®Google Scholar
• Lafarga M, Berciano MT, Garcia-Segura LM, et al. Acute osmotic/stress stimuli induce a transient decrease of transcriptional activity in the neurosecretory neurons of supraoptic nuclei. J Neurocytol. 1998;27(4):205–217. doi: 10.1023/A:1006937032068
   PubMedGoogle Scholar
• Boudonck K, Dolan L, Shaw PJ. Coiled body numbers in the Arabidopsis root epidermis are regulated by cell type, developmental stage and cell cycle parameters. J Cell Sci. 1998;111(24):3687–3694. doi: 10.1242/jcs.111.24.3687
   PubMedGoogle Scholar
• Ferreira J, Carmo-Fonseca M. The biogenesis of the coiled body during early mouse development. Development. 1995;121(2):601–612. doi: 10.1242/dev.121.2.601
   PubMed Web of Science ®Google Scholar
• Strzelecka M, Oates AC, Neugebauer KM. Dynamic control of Cajal body number during zebrafish embryogenesis. Nucleus. 2010;1(1):96–108. doi: 10.4161/nucl.1.1.10680
   PubMed Web of Science ®Google Scholar
• Strzelecka M, Trowitzsch S, Weber G, et al. Coilin-dependent snRNP assembly is essential for zebrafish embryogenesis. Nat Struct Mol Biol. 2010;17(4):403–409. doi: 10.1038/nsmb.1783
   PubMed Web of Science ®Google Scholar
• Stanek D, Fox AH. Nuclear bodies: news insights into structure and function. Curr Opin Cell Biol. 2017;46:94–101. doi: 10.1016/j.ceb.2017.05.001
   PubMed Web of Science ®Google Scholar
• Shin Y, Brangwynne CP. Liquid phase condensation in cell physiology and disease. Science. 2017;357(6357). doi: 10.1126/science.aaf4382
   PubMed Web of Science ®Google Scholar
• Tucker KE, Berciano MT, Jacobs EY, et al. Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy gene product. J Cell Bio. 2001;154(2):293–308. doi: 10.1083/jcb.200104083
   PubMed Web of Science ®Google Scholar
• Liu JL, Wu Z, Nizami Z, et al. Coilin is essential for Cajal body organization in Drosophila melanogaster. Mol Biol Cell. 2009;20(6):1661–1670. doi: 10.1091/mbc.e08-05-0525
   PubMed Web of Science ®Google Scholar
• Chen Y, Deng Z, Jiang S, et al. Human cells lacking coilin and Cajal bodies are proficient in telomerase assembly, trafficking and telomere maintenance. Nucleic Acids Res. 2015;43(1):385–395. doi: 10.1093/nar/gku1277
   PubMed Web of Science ®Google Scholar
• Basello DA, Matera AG, Stanek D. A point mutation in human coilin prevents Cajal body formation. J Cell Sci. 2022;135(8). doi: 10.1242/jcs.259587
   PubMed Web of Science ®Google Scholar
• Collier S, Pendle A, Boudonck K, et al. A distant coilin homologue is required for the formation of Cajal bodies in Arabidopsis. Mol Biol Cell. 2006;17(7):2942–2951. doi: 10.1091/mbc.e05-12-1157
   PubMed Web of Science ®Google Scholar
• Hebert MD, Matera AG, Silver PA. Self-association of coilin reveals a common theme in nuclear body localization. Mol Biol Cell. 2000;11(12):4159–4171. doi: 10.1091/mbc.11.12.4159
   PubMed Web of Science ®Google Scholar
• Courchaine E, Gelles-Watnick S, Machyna M, et al. The coilin N-terminus mediates multivalent interactions between coilin and Nopp140 to form and maintain Cajal bodies. Nat Commun. 2022;13(1):6005. doi: 10.1038/s41467-022-33434-2
   PubMed Web of Science ®Google Scholar
• Stanek D, Neugebauer KM. Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer. J Cell Bio. 2004;166(7):1015–1025. doi: 10.1083/jcb.200405160
   PubMed Web of Science ®Google Scholar
• Sleeman J, Lyon CE, Platani M, et al. Dynamic interactions between splicing snRnps, coiled bodies and nucleoli revealed using snRNP protein fusions to the green fluorescent protein. Exp Cell Res. 1998;243(2):290–304. doi: 10.1006/excr.1998.4135
   PubMed Web of Science ®Google Scholar
• Lyon CE, Bohmann K, Sleeman J, et al. Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus. Exp Cell Res. 1997;230(1):84–93. doi: 10.1006/excr.1996.3380
   PubMed Web of Science ®Google Scholar
• Broome HJ, Carrero ZI, Douglas HE, et al. Phosphorylation regulates coilin activity and RNA association. Biol Open. 2013;2(4):407–415. doi: 10.1242/bio.20133863
   PubMed Web of Science ®Google Scholar
• Hearst SM, Gilder AS, Negi SS, et al. Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines. J Cell Sci. 2009;122(11):1872–1881. doi: 10.1242/jcs.044040
   PubMed Web of Science ®Google Scholar
• Carrero ZI, Velma V, Douglas HE, et al. Coilin phosphomutants disrupt Cajal body formation, reduce cell proliferation and produce a distinct coilin degradation product. PLoS One. 2011;6(10):e25743. doi: 10.1371/journal.pone.0025743
   PubMed Web of Science ®Google Scholar
• Hebert MD, Poole AR. Towards an understanding of regulating Cajal body activity by protein modification. RNA Biol. 2017;14(6):761–778. doi: 10.1080/15476286.2016.1243649
   PubMed Web of Science ®Google Scholar
• Berchtold D, Battich N, Pelkmans L. A systems-level study reveals regulators of membrane-less organelles in human cells. Mol Cell. 2018;72(6):1035–49 e5. doi: 10.1016/j.molcel.2018.10.036
   PubMed Web of Science ®Google Scholar
• Jonik-Nowak B, Menneteau T, Fesquet D, et al. PIP30/FAM192A is a novel regulator of the nuclear proteasome activator PA28γ. Proc Natl Acad Sci U S A. 2018;115(28):E6477–E86. doi: 10.1073/pnas.1722299115
   PubMed Web of Science ®Google Scholar
• Cantarero L, Sanz-Garcia M, Vinograd-Byk H, et al. VRK1 regulates Cajal body dynamics and protects coilin from proteasomal degradation in cell cycle. Sci Rep. 2015;5(1):10543. doi: 10.1038/srep10543
   PubMedGoogle Scholar
• Niu H, Zhao M, Huang J, et al. UHMK1-dependent phosphorylation of Cajal body protein coilin alters 5-FU sensitivity in colon cancer cells. Cell Commun Signal. 2022;20(1):18. doi: 10.1186/s12964-022-00820-8
   PubMed Web of Science ®Google Scholar
• Martin-Doncel E, Rojas AM, Cantarero L, et al. VRK1 functional insufficiency due to alterations in protein stability or kinase activity of human VRK1 pathogenic variants implicated in neuromotor syndromes. Sci Rep. 2019;9(1):13381. doi: 10.1038/s41598-019-49821-7
   PubMedGoogle Scholar
• Liu J, Hebert MD, Ye Y, et al. Cell cycle-dependent localization of the CDK2-cyclin E complex in Cajal (coiled) bodies. J Cell Sci. 2000;113(Pt 9):1543–1552. doi: 10.1242/jcs.113.9.1543
   PubMed Web of Science ®Google Scholar
• Bellini M, Gall JG, Blackburn EA. Coilin can form a complex with the U7 small nuclear ribonucleoprotein. Mol Biol Cell. 1998;9(10):2987–3001. doi: 10.1091/mbc.9.10.2987
   PubMed Web of Science ®Google Scholar
• Makarov V, Rakitina D, Protopopova A, et al. Plant coilin: structural characteristics and RNA-binding properties. PLoS One. 2013;8(1):e53571. doi: 10.1371/journal.pone.0053571
   PubMed Web of Science ®Google Scholar
• Broome HJ, Hebert MD. Coilin displays differential affinity for specific RNAs in vivo and is linked to telomerase RNA biogenesis. J Mol Biol. 2013;425(4):713–724. doi: 10.1016/j.jmb.2012.12.014
   PubMed Web of Science ®Google Scholar
• Machyna M, Neugebauer KM, Stanek D. Coilin: the first 25 years. RNA Biol. 2015;12(6):590–596. doi: 10.1080/15476286.2015.1034923
   PubMed Web of Science ®Google Scholar
• Hebert MD, Szymczyk PW, Shpargel KB, et al. Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein. Genes Dev. 2001;15(20):2720–2729. doi: 10.1101/gad.908401
   PubMed Web of Science ®Google Scholar
• Shanbhag R, Kurabi A, Kwan JJ, et al. Solution structure of the carboxy-terminal Tudor domain from human Coilin. FEBS Lett. 2010;584(20):4351–4356. doi: 10.1016/j.febslet.2010.09.034
   PubMed Web of Science ®Google Scholar
• Courchaine EM, Barentine AES, Straube K, et al. DMA-tudor interaction modules control the specificity of in vivo condensates. Cell. 2021;184(14):3612–3625.e17. doi: 10.1016/j.cell.2021.05.008
   PubMed Web of Science ®Google Scholar
• Meister G, Eggert C, Buhler D, et al. Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol. 2001;11(24):1990–1994. doi: 10.1016/S0960-9822(01)00592-9
   PubMed Web of Science ®Google Scholar
• Meister G, Eggert C, Fischer U. SMN-mediated assembly of RNPs: a complex story. Trends Cell Biol. 2002;12(10):472–478. doi: 10.1016/S0962-8924(02)02371-1
   PubMed Web of Science ®Google Scholar
• Xu H, Pillai RS, Azzouz TN, et al. The C-terminal domain of coilin interacts with Sm proteins and U snRNPs. Chromosoma. 2005;114(3):155–166. doi: 10.1007/s00412-005-0003-y
   PubMed Web of Science ®Google Scholar
• Shpargel KB, Ospina JK, Tucker KE, et al. Control of Cajal body number is mediated by the coilin C-terminus. J Cell Sci. 2003;116(2):303–312. doi: 10.1242/jcs.00211
   PubMed Web of Science ®Google Scholar
• Sleeman JE, Ajuh P, Lamond AI. snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN. J Cell Sci. 2001;114(24):4407–4419. doi: 10.1242/jcs.114.24.4407
   PubMed Web of Science ®Google Scholar
• Novotny I, Malinova A, Stejskalova E, et al. SART3-dependent accumulation of incomplete spliceosomal snRNPs in Cajal bodies. Cell Rep. 2015;10(3):429–440. doi: 10.1016/j.celrep.2014.12.030
   PubMed Web of Science ®Google Scholar
• Roithova A, Klimesova K, Panek J, et al. The Sm-core mediates the retention of partially-assembled spliceosomal snRnps in Cajal bodies until their full maturation. Nucleic Acids Res. 2018;46(7):3774–3790. doi: 10.1093/nar/gky070
   PubMed Web of Science ®Google Scholar
• Kaiser TE, Intine RV, Dundr M. De Novo formation of a subnuclear body. Science. 2008;322(5908):1713–1717. doi: 10.1126/science.1165216
   PubMed Web of Science ®Google Scholar
• Takata H, Nishijima H, Maeshima K, et al. The Integrator complex is required for integrity of Cajal bodies. J Cell Sci. 2012;125(1):166–175. doi: 10.1242/jcs.090837
   PubMed Web of Science ®Google Scholar
• Albrecht TR, Shevtsov SP, Wu Y, et al. Integrator subunit 4 is a ‘symplekin-like’ scaffold that associates with INTS9/11 to form the integrator cleavage module. Nucleic Acids Res. 2018;46(8):4241–4255. doi: 10.1093/nar/gky100
   PubMed Web of Science ®Google Scholar
• Lemm I, Girard C, Kuhn AN, et al. Ongoing U snRNP biogenesis is required for the integrity of Cajal bodies. Mol Biol Cell. 2006;17(7):3221–3231. doi: 10.1091/mbc.e06-03-0247
   PubMed Web of Science ®Google Scholar
• Moreno-Castro C, Prieto-Sanchez S, Sanchez-Hernandez N, et al. Role for the splicing factor TCERG1 in Cajal body integrity and snRNP assembly. J Cell Sci. 2019;132. doi: 10.1242/jcs.232728
   Web of Science ®Google Scholar
• Cihlarova Z, Kubovciak J, Sobol M, et al. BRAT1 links integrator and defective RNA processing with neurodegeneration. Nat Commun. 2022;13(1):5026. doi: 10.1038/s41467-022-32763-6
   PubMed Web of Science ®Google Scholar
• Girard C, Neel H, Bertrand E, et al. Depletion of SMN by RNA interference in HeLa cells induces defects in Cajal body formation. Nucleic Acids Res. 2006;34(10):2925–2932. doi: 10.1093/nar/gkl374
   PubMed Web of Science ®Google Scholar
• Mahmoudi S, Henriksson S, Weibrecht I, et al. WRAP53 is essential for Cajal body formation and for targeting the survival of motor neuron complex to Cajal bodies. PLoS Biol. 2010;8(11):e1000521. doi: 10.1371/journal.pbio.1000521
   PubMed Web of Science ®Google Scholar
• Shpargel KB, aG M. Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins. Proc Natl Acad Sci U S A. 2005;102(48):17372–17377. doi: 10.1073/pnas.0508947102
   PubMed Web of Science ®Google Scholar
• Zhai F, Wang J, Luo X, et al. Roles of NOLC1 in cancers and viral infection. J Cancer Res Clin Oncol. 2023;149(12):10593–10608. doi: 10.1007/s00432-023-04934-5
   PubMed Web of Science ®Google Scholar
• Meier UT, Blobel G. NAP57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria. J Cell Bio. 1994;127(6):1505–1514. doi: 10.1083/jcb.127.6.1505
   PubMed Web of Science ®Google Scholar
• Yang Y, Isaac C, Wang C, et al. Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140. Mol Biol Cell. 2000;11(2):567–577. doi: 10.1091/mbc.11.2.567
   PubMed Web of Science ®Google Scholar
• Wang C, Query CC, Meier UT. Immunopurified small nucleolar ribonucleoprotein particles pseudouridylate rRNA independently of their association with phosphorylated Nopp140. Mol Cell Biol. 2002;22(24):8457–8466. doi: 10.1128/MCB.22.24.8457-8466.2002
   PubMed Web of Science ®Google Scholar
• Isaac C, Yang Y, Meier UT. Nopp140 functions as a molecular link between the nucleolus and the coiled bodies. J Cell Bio. 1998;142(2):319–329. doi: 10.1083/jcb.142.2.319
   PubMed Web of Science ®Google Scholar
• Bizarro J, Deryusheva S, Wacheul L, et al. Nopp140-chaperoned 2´-O-methylation of small nuclear RNAs in Cajal bodies ensures splicing fidelity. Genes Dev. 2021;35(15–16):1123–1141. doi: 10.1101/gad.348660.121
   PubMed Web of Science ®Google Scholar
• Riback JA, Zhu L, Ferrolino MC, et al. Composition-dependent thermodynamics of intracellular phase separation. Nature. 2020;581(7807):209–214. doi: 10.1038/s41586-020-2256-2
   PubMed Web of Science ®Google Scholar
• Klingauf M, Stanek D, Neugebauer KM, et al. Enhancement of U4/U6 small nuclear ribonucleoprotein particle association in Cajal bodies predicted by mathematical modeling. Mol Biol Cell. 2006;17(12):4972–4981. doi: 10.1091/mbc.e06-06-0513
   PubMed Web of Science ®Google Scholar
• Stanek D, Pridalova-Hnilicova J, Novotny I, et al. Spliceosomal small nuclear ribonucleoprotein particles repeatedly cycle through Cajal bodies. Mol Biol Cell. 2008;19(6):2534–2543. doi: 10.1091/mbc.e07-12-1259
   PubMed Web of Science ®Google Scholar
• Novotny I, Blazikova M, Stanek D, et al. In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies. Mol Biol Cell. 2011;22(4):513–523. doi: 10.1091/mbc.e10-07-0560
   PubMed Web of Science ®Google Scholar
• Schaffert N, Hossbach M, Heintzmann R, et al. RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 di-snRnps in Cajal bodies. EMBO J. 2004;23(15):3000–3009. doi: 10.1038/sj.emboj.7600296
   PubMed Web of Science ®Google Scholar
• Walker MP, Tian L, Matera AG, et al. Reduced viability, fertility and fecundity in mice lacking the Cajal body marker protein, coilin. PLoS One. 2009;4(7):e6171. doi: 10.1371/journal.pone.0006171
   PubMed Web of Science ®Google Scholar
• Abulfaraj AA, Alhoraibi HM, Mariappan K, et al. Analysis of the Arabidopsis coilin mutant reveals a positive role of AtCOILIN in plant immunity. Plant Physiol. 2022;190(1):745–761. doi: 10.1093/plphys/kiac280
   PubMed Web of Science ®Google Scholar
• Deryusheva S, Gall JG, Matera AG. Small Cajal body–specific RNAs of Drosophila function in the absence of Cajal bodies. Mol Biol Cell. 2009;20(24):5250–5259. doi: 10.1091/mbc.e09-09-0777
   PubMed Web of Science ®Google Scholar
• Bizarro J, Dodre M, Huttin A, et al. NUFIP and the HSP90/R2TP chaperone bind the SMN complex and facilitate assembly of U4-specific proteins. Nucleic Acids Res. 2015;43(18):8973–8989. doi: 10.1093/nar/gkv809
   PubMed Web of Science ®Google Scholar
• Nesic D, Tanackovic G, Kramer A. A role for Cajal bodies in the final steps of U2 snRNP biogenesis. J Cell Sci. 2004;117(19):4423–4433. doi: 10.1242/jcs.01308
   PubMed Web of Science ®Google Scholar
• Tanackovic G, Kramer A. Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo. Mol Biol Cell. 2005;16(3):1366–1377. doi: 10.1091/mbc.e04-11-1034
   PubMed Web of Science ®Google Scholar
• Malinova A, Cvackova Z, Mateju D, et al. Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones. J Cell Bio. 2017;216(6):1579–1596. doi: 10.1083/jcb.201701165
   PubMed Web of Science ®Google Scholar
• Klimesova K, Vojackova J, Radivojevic N, et al. TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation. Nat Commun. 2021;12(1):3646. doi: 10.1038/s41467-021-23934-y
   PubMed Web of Science ®Google Scholar
• Klimesova K, Petrzilkova H, Barinka C, et al. SART3 associates with a post-splicing complex. J Cell Sci. 2023;136(2). doi: 10.1242/jcs.260380
   PubMed Web of Science ®Google Scholar
• Zhu Y, Tomlinson RL, Lukowiak AA, et al. Telomerase RNA accumulates in Cajal bodies in human cancer cells. Mol Biol Cell. 2004;15(1):81–90. doi: 10.1091/mbc.e03-07-0525
   PubMed Web of Science ®Google Scholar
• Jady BE, Bertrand E, Kiss T. Human telomerase RNA and box H/ACA scaRnas share a common Cajal body–specific localization signal. J Cell Bio. 2004;164(5):647–652. doi: 10.1083/jcb.200310138
   PubMed Web of Science ®Google Scholar
• Venteicher AS, Abreu EB, Meng Z, et al. A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis. Science. 2009;323(5914):644–648. doi: 10.1126/science.1165357
   PubMed Web of Science ®Google Scholar
• Cristofari G, Adolf E, Reichenbach P, et al. Human telomerase RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation. Mol Cell. 2007;27(6):882–889. doi: 10.1016/j.molcel.2007.07.020
   PubMed Web of Science ®Google Scholar
• Zhong F, Savage SA, Shkreli M, et al. Disruption of telomerase trafficking by TCAB1 mutation causes dyskeratosis congenita. Genes Dev. 2011;25(1):11–16. doi: 10.1101/gad.2006411
   PubMed Web of Science ®Google Scholar
• Stern JL, Zyner KG, Pickett HA, et al. Telomerase recruitment requires both TCAB1 and Cajal bodies independently. Mol Cell Biol. 2012;32(13):2384–2395. doi: 10.1128/MCB.00379-12
   PubMed Web of Science ®Google Scholar
• Tomlinson RL, Li J, Culp BR, et al. A Cajal body-independent pathway for telomerase trafficking in mice. Exp Cell Res. 2010;316(17):2797–2809. doi: 10.1016/j.yexcr.2010.07.001
   PubMed Web of Science ®Google Scholar
• Vogan JM, Zhang X, Youmans DT, et al. Minimized human telomerase maintains telomeres and resolves endogenous roles of H/ACA proteins, TCAB1, and Cajal bodies. Elife. 2016;5. doi: 10.7554/eLife.18221
   PubMed Web of Science ®Google Scholar
• Buemi V, Schillaci O, Santorsola M, et al. TGS1 mediates 2,2,7-trimethyl guanosine capping of the human telomerase RNA to direct telomerase dependent telomere maintenance. Nat Commun. 2022;13(1):2302. doi: 10.1038/s41467-022-29907-z
   PubMed Web of Science ®Google Scholar
• Chen L, Roake CM, Galati A, et al. Loss of human TGS1 hypermethylase promotes increased telomerase RNA and telomere elongation. Cell Rep. 2020;30(5):1358–72 e5. doi: 10.1016/j.celrep.2020.01.004
   PubMed Web of Science ®Google Scholar
• Kim NK, Theimer CA, Mitchell JR, et al. Effect of pseudouridylation on the structure and activity of the catalytically essential P6.1 hairpin in human telomerase RNA. Nucleic Acids Res. 2010;38(19):6746–6756. doi: 10.1093/nar/gkq525
   PubMed Web of Science ®Google Scholar
• Rudzka M, Wroblewska-Ankiewicz P, Majewska K, et al. Functional nuclear retention of pre-mRNA involving Cajal bodies during meiotic prophase in European larch (Larix decidua). Plant Cell. 2022;34(6):2404–2423. doi: 10.1093/plcell/koac091
   PubMed Web of Science ®Google Scholar
• Shaw J, Love AJ, Makarova SS, et al. Coilin, the signature protein of Cajal bodies, differentially modulates the interactions of plants with viruses in widely different taxa. Nucleus. 2014;5(1):85–94. doi: 10.4161/nucl.28315
   PubMed Web of Science ®Google Scholar
• Love AJ, Yu C, Petukhova NV, et al. Cajal bodies and their role in plant stress and disease responses. RNA Biol. 2017;14(6):779–790. doi: 10.1080/15476286.2016.1243650
   PubMed Web of Science ®Google Scholar
• Kotova E, Jarnik M, Tulin AV, et al. Poly (ADP-ribose) polymerase 1 is required for protein localization to Cajal body. PLoS Genet. 2009;5(2):e1000387. doi: 10.1371/journal.pgen.1000387
   PubMed Web of Science ®Google Scholar
• Spechenkova N, Samarskaya VO, Kalinina NO, et al. Plant Poly(ADP-Ribose) polymerase 1 is a potential mediator of cross-talk between the Cajal body protein coilin and salicylic acid-mediated antiviral defence. Viruses. 2023;15(6):15. doi: 10.3390/v15061282
   Web of Science ®Google Scholar
• Shaw J, Yu C, Makhotenko AV, et al. Interaction of a plant virus protein with the signature Cajal body protein coilin facilitates salicylic acid-mediated plant defence responses. New Phytol. 2019;224(1):439–453. doi: 10.1111/nph.15994
   PubMed Web of Science ®Google Scholar
• Petrovska B, Sebela M, Dolezel J. Inside a plant nucleus: discovering the proteins. J Exp Bot. 2015;66(6):1627–1640. doi: 10.1093/jxb/erv041
   PubMed Web of Science ®Google Scholar