Carvalho T, Almeida F, Calapez A, Lafarga M, Berciano MT, Carmo-Fonseca M. (1999) The spinal muscular atrophy disease gene product, SMN: A link between snRNP biogenesis and the Cajal (coiled) body. J Cell Biol 147:715-728.
Fischer U, Liu Q, and Dreyfuss G. (1997) The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell 90:1023-1029.
Frey MR and Matera AG (2001) RNA-mediated interaction of Cajal bodies and U2 snRNA genes . J. Cell Biol. 154:499-509.
Gall, J. G. (2000) Cajal bodies: the first 1000 years. Annu. Rev. Cell Dev. Biol. 16:273-300.
Herbert MD, Szymczyk PW, Shpargel KB and Matera AG (2001) Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein . Genes Dev. 15:2720-2729.
Herbert MD, Shpargel KB, Ospina JK, Tucker KE and Matera AG (2002) Coilin methylation regulates nuclear body formation. Dev. Cell 3: 329-37
Jacobs EY, Frey MR, Wu W, Ingledue TC, Gebuhr TC, Gao L, Marzluff WF, and Matera AG (1999) 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 10:1653-1663.
Ogg SC. and Lamond AI. (2002) Cajal bodies and coilin - moving towards function. J. Cell Biol. 159:17-21.
Paushkin, S, Gubitz AK, Massenet S and Dreyfuss G (2002) The SMN complex, an assemblysome of ribonucleoproteins. Curr. Opin. Cell Biol. 14:305-312.
Platini M, Goldberg I, Lamond AI and Swedlow JR (2002) Cajal body dynamics and association with chromatin are ATP-dependent. Nat. Cell Biol. 4:502-508.
Shopland LS, Byron M, Stein JL, Lian JB, Stein GS and Lawrence JB (2001) Replication-dependent histone gene expression is related to Cajal body (CB) association but does not require sustained CB contact. Mol. Biol. Cell, 12:565-576.
Sleeman JE, and Lamond AI.(1999) Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway. Curr. Biol. 9:1065-1074.
Tucker KE, Berciano MT, Jacobs EY, LePage DF, Shpargel KB, Rossire JJ, Chan EK, Lafarga M, Conlon Ra and Matera AG (2001) Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy gene product. J. Cell Biol. 154:293-307.
Yamada M, Sato T, Shimohata T, Hayashi S, Igarashi S, Tsuji S, Takahashi H. Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases. (2001). Am J Pathol 2001 Nov;159(5):1785-95
Polak PE, Simone F, Kaberlein JJ, Luo RT, Thirman MJ. (2003) ELL and EAF1 are Cajal Body Components That Are Disrupted in MLL-ELL Leukemia. Mol Biol Cell. 14:1517-1528.
Ровно 100 лет тому назад испанский нейробиолог Santiago Ramon y Cajal описал новый тип органелл в ядрах нейронов позвоночных. Ныне называемые тельцами Кахаля (Cajal) эти органеллы появляются во многих типах елеток у широкго круга животных и растений. Недавние исследования показали, что тельца Кахаля выполняют мнгочисленные роли по сборке и/или модификации кухни (machinery) ядерной транскрипции и процессинга РНК. (THE CENTENNIAL OF THE CAJAL BODY Joseph G. GallNature Reviews Molecular Cell Biology4, No 12, 975 -980 (2003); doi:10.1038/nrm1262)
Elena Kiseleva (Institute of Cytology and Genetics, Russia; Paterson Institute for Cancer Research, UK (ekiseleva@picr.man.ac.uk)) продемонстрировала комплексы ядерных пор и тельца Кахаля, связанные с экстенсивной актин-зависимой филаментозной сетью в ядрах ооцитов Xenopus laevis.
Purple и pink псевдо-окрашивание представляет собой анти-coilin-меченные тельца Кахаля и филаментозную сеть, соотв. Еmission scanning electron microscope (DS 130F, Topcon). Bar, 167 nm.
Cajal Bodies
Plant and human nuclei contain between 0 - 10 Cajal bodies (previously called coiled bodies) of ~ 0.1-2.0 µM in diameter (reviewed in Gall, 2000). They are most adundant in very transcriptionally active and proliferating cells, and are less abundant in, or absent from, some primary cells and tissues. Cajal bodies are often found in the vicinity of . A major component of Cajal bodies is the protein and upon transcriptional inhibition Cajal bodies disappear and coilin is then found in perinucleolar caps (Ogg and Lamond, 2002). Cajal bodies are also very dynamic, often being seen to split into two, or to fuse with each other (Platani et al., 2002).
Gems
Gems are characterised by their association with the proteins and . They are often found paired or juxtaposed to Cajal bodies and though once considered two separate but related nuclear bodies, Gems and Cajal bodies are now considered to be two manifestations of the same structure. Communication between Cajal bodies and Gems is mediated by coilin (Herbert at al., 2001). Coilin contains symmetrically dimethylated arginine residues (sDMAs) within an RG box, which modulate its affinity for SMN. Inhibition of the methylation, or mutation of the RG box decreases the interaction of coilin with SMN, resulting in the formation of gems that are separate from Cajal bodies. When coilin is methylated Cajal bodies and gems are coincident (Herbert et al., 2002) .
Function of Cajal bodies and Gems
Cajal bodies are involved in snRNP biogenesis and in the trafficking of snoRNPs and snRNPs, which move through the Cajal body en route to or (respectively) (Sleeman and Lamond 1999). For example, the spliceosomal U1, U2, U4/U6 and U5 snRNPs localise to these bodies, as well as the U7 snRNP involved in histone 3'-end processing. The U3 and U8 snoRNPs, involved in pre-rRNA processing, also localise to Cajal bodies (Gall, 2000). In addition, several gene loci, including histone (Shopland et al., 2001) , U1, U2, U3, U4, U11 and U12 genes (Jacobs et al., 1999) appear to associate preferentially with Cajal bodies in a manner that is dependent on expression of these loci (Frey and Matera, 2001) .
SMN and an associated protein form a complex that plays an essential role in cytoplasmic snRNP biogenesis (Fischer et al., 1997). As with coilin, sDMA modification of Sm snRNPs enhances their binding to the SMN complex (Paushkin et al., 2002). SnRNPs and snoRNPs are assembled in the cytoplasm, imported into the nucleus and then further matured. Cajal bodies appear to contain newly imported RNP particles that then become concentrated into splicing speckles or nucleoli respectively. It is likely that Cajal bodies are sites at which snRNA modification occurs (Ogg and Lamond, 2002). Cajal bodies contain a putative RNA methyltransferase. Mice lacking have only residual Cajal bodies that do not recruit Sm snRNPs and SMN, and the animals have reduced viability (Tucker et al., 2001) .
Cajal bodies/Gems and Disease
Loss of function mutations in the survival of motor neurons (SMN) gene are found in (Carvalho et al., 1999). Therefore, defects in spliceosomal snRNP assembly may underlie the development of spinal musclular atrophy. The nuclear inclusions seen in neurons from individuals with Huntington's disease and other CAG repeat diseases that result in polyglutamate expansions are often associated with Cajal bodies (Yamada et al., 2001). Cajal bodies are also disrupted in MLL-ELL leukaemia in which the Cajal body protein is fused to (Polak et al., 2003) .
Published Movies of Cajal body dynamics
The Movement of Coiled Bodies Visualized in Living Plant Cells by the Green Fluorescent Protein". K Boudonck et al. (1999).
In Vivo Analysis of Cajal Body Movement, Separation, and Joining in Live Human Cells. M. Platani et al. (2000).
Lamond lab Cajal body images and movies - - - movie - images from the Lamond lab (shows accumulation of coilin in the nucleolus upon okadaic acid treatment).
Cajal Bodies
