SYMPK explained
Symplekin is a protein that in humans is encoded by the SYMPK gene.[1] [2]
Function
This gene encodes a nuclear protein that functions in the regulation of polyadenylation and promotes gene expression. The protein forms a high-molecular weight complex with components of the polyadenylation machinery. It is thought to serve as a scaffold for recruiting regulatory factors to the polyadenylation complex. It also participates in 3'-end maturation of histone mRNAs, which do not undergo polyadenylation. The protein also localizes to the cytoplasmic plaques of tight junctions in some cell types.[2]
Interactions
SYMPK has been shown to interact with CSTF2,[3] HSF1[4] and Oct4[5]
Further reading
- Keon BH, Schäfer S, Kuhn C, Grund C, Franke WW . Symplekin, a novel type of tight junction plaque protein . The Journal of Cell Biology . 134 . 4 . 1003–18 . Aug 1996 . 8769423 . 2120966 . 10.1083/jcb.134.4.1003 .
- Alwazzan M, Hamshere MG, Lennon GG, Brook JD . Six transcripts map within 200 kilobases of the myotonic dystrophy expanded repeat . Mammalian Genome . 9 . 6 . 485–7 . Jun 1998 . 9585442 . 10.1007/s003359900804 . 319161 .
- Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME . Huntingtin interacts with a family of WW domain proteins . Human Molecular Genetics . 7 . 9 . 1463–74 . Sep 1998 . 9700202 . 10.1093/hmg/7.9.1463 . free .
- Paffenholz R, Kuhn C, Grund C, Stehr S, Franke WW . The arm-repeat protein NPRAP (neurojungin) is a constituent of the plaques of the outer limiting zone in the retina, defining a novel type of adhering junction . Experimental Cell Research . 250 . 2 . 452–64 . Aug 1999 . 10413599 . 10.1006/excr.1999.4534 .
- Takagaki Y, Manley JL . Complex protein interactions within the human polyadenylation machinery identify a novel component . Molecular and Cellular Biology . 20 . 5 . 1515–25 . Mar 2000 . 10669729 . 85326 . 10.1128/MCB.20.5.1515-1525.2000 .
- Langbein L, Pape UF, Grund C, Kuhn C, Praetzel S, Moll I, Moll R, Franke WW . Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely packed cell formations of stratified epithelia and squamous cell carcinomas . European Journal of Cell Biology . 82 . 8 . 385–400 . Aug 2003 . 14533737 . 10.1078/0171-9335-00330 .
- Xing H, Mayhew CN, Cullen KE, Park-Sarge OK, Sarge KD . HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin . The Journal of Biological Chemistry . 279 . 11 . 10551–5 . Mar 2004 . 14707147 . 10.1074/jbc.M311719200 . free .
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP . Large-scale characterization of HeLa cell nuclear phosphoproteins . Proceedings of the National Academy of Sciences of the United States of America . 101 . 33 . 12130–5 . Aug 2004 . 15302935 . 514446 . 10.1073/pnas.0404720101 . 2004PNAS..10112130B . free .
- Barnard DC, Ryan K, Manley JL, Richter JD . Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation . Cell . 119 . 5 . 641–51 . Nov 2004 . 15550246 . 10.1016/j.cell.2004.10.029 . 8289230 . free .
- Kolev NG, Steitz JA . Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs . Genes & Development . 19 . 21 . 2583–92 . Nov 2005 . 16230528 . 1276732 . 10.1101/gad.1371105 .
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S . Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes . Genome Research . 16 . 1 . 55–65 . Jan 2006 . 16344560 . 1356129 . 10.1101/gr.4039406 .
- Kavanagh E, Buchert M, Tsapara A, Choquet A, Balda MS, Hollande F, Matter K . Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin . Journal of Cell Science . 119 . Pt 24 . 5098–105 . Dec 2006 . 17158914 . 10.1242/jcs.03297 . 8702837 . free .
Notes and References
- Ueki K, Ramaswamy S, Billings SJ, Mohrenweiser HW, Louis DN . Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA sequence of the human symplekin gene . Somatic Cell and Molecular Genetics . 23 . 3 . 229–31 . May 1997 . 9330635 . 10.1007/BF02721375 . 24956684 .
- Web site: Entrez Gene: SYMPK symplekin.
- Takagaki Y, Manley JL . Complex protein interactions within the human polyadenylation machinery identify a novel component . Molecular and Cellular Biology . 20 . 5 . 1515–25 . Mar 2000 . 10669729 . 85326 . 10.1128/MCB.20.5.1515-1525.2000 .
- Xing H, Mayhew CN, Cullen KE, Park-Sarge OK, Sarge KD . HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin . The Journal of Biological Chemistry . 279 . 11 . 10551–5 . Mar 2004 . 14707147 . 10.1074/jbc.M311719200 . free .
- Yu J, Lu W, Ge T, et al., (2019). "Interaction Between Sympk and Oct4 Promotes Mouse Embryonic Stem Cell Proliferation". STEM CELLS;37(6): 743-753 https://doi.org/10.1002/stem.2992