SEPT2
Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.[1][2]
Function
SEPT2 can hetero-oligomerize with SEPT6 and SEPT7 to form filaments.[3] SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain.[3] Knockdown of SEPT2, SEPT6, and SEPT7 in causes actin stress fibers to disintegrate and cells to lose polarity. Septins, SOCS7, and NCK1 are part of a signaling pathway that couples regulation of the DNA damage response to the cytoskeleton.[4]
Interactions
SEPT2 has been shown to interact with:
References
- ↑ "Entrez Gene: SEPT2 septin 2".
- ↑ Mori T, Miura K, Fujiwara T, Shin S, Inazawa J, Nakamura Y (1996). "Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3, CDC10, CDC11, and CDC12, and mouse Diff6". Cytogenet. Cell Genet. 73 (3): 224–7. doi:10.1159/000134343. PMID 8697812.
- 1 2 Low C, Macara IG (October 2006). "Structural analysis of septin 2, 6, and 7 complexes". J. Biol. Chem. 281 (41): 30697–706. doi:10.1074/jbc.M605179200. PMID 16914550.
- ↑ Kremer BE, Adang LA, Macara IG (September 2007). "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7". Cell 130 (5): 837–50. doi:10.1016/j.cell.2007.06.053. PMC 2085444. PMID 17803907.
- 1 2 3 Surka MC, Tsang CW, Trimble WS (Oct 2002). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis". Mol. Biol. Cell 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. PMC 129964. PMID 12388755.
- ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Further reading
- Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
- Mori T, Miura K, Fujiwara T, Shin S, Inazawa J, Nakamura Y (1996). "Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3, CDC10, CDC11, and CDC12, and mouse Diff6.". Cytogenet. Cell Genet. 73 (3): 224–7. doi:10.1159/000134343. PMID 8697812.
- Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, Hiraoka Y, Noda M (1997). "Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures.". Genes Dev. 11 (12): 1535–47. doi:10.1101/gad.11.12.1535. PMID 9203580.
- Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments.". Neuron 20 (6): 1111–22. doi:10.1016/S0896-6273(00)80493-6. PMID 9655500.
- Kinoshita A, Kinoshita M, Akiyama H, Tomimoto H, Akiguchi I, Kumar S, Noda M, Kimura J (1998). "Identification of septins in neurofibrillary tangles in Alzheimer's disease.". Am. J. Pathol. 153 (5): 1551–60. doi:10.1016/S0002-9440(10)65743-4. PMC 1853406. PMID 9811347.
- "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
- Beites CL, Xie H, Bowser R, Trimble WS (1999). "The septin CDCrel-1 binds syntaxin and inhibits exocytosis.". Nat. Neurosci. 2 (5): 434–9. doi:10.1038/8100. PMID 10321247.
- Hoja MR, Wahlestedt C, Höög C (2000). "A visual intracellular classification strategy for uncharacterized human proteins.". Exp. Cell Res. 259 (1): 239–46. doi:10.1006/excr.2000.4948. PMID 10942595.
- Sakai K, Kurimoto M, Tsugu A, Hubbard SL, Trimble WS, Rutka JT (2003). "Expression of Nedd5, a mammalian septin, in human brain tumors.". J. Neurooncol. 57 (3): 169–77. doi:10.1023/A:1015721801075. PMID 12125979.
- Surka MC, Tsang CW, Trimble WS (2003). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis.". Mol. Biol. Cell 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. PMC 129964. PMID 12388755.
- Sheffield PJ, Oliver CJ, Kremer BE, Sheng S, Shao Z, Macara IG (2003). "Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments.". J. Biol. Chem. 278 (5): 3483–8. doi:10.1074/jbc.M209701200. PMID 12446710.
- Vega IE, Hsu SC (2003). "The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells.". NeuroReport 14 (1): 31–7. doi:10.1097/01.wnr.0000050304.92401.50. PMID 12544826.
- Koshelev YA, Kiselev SL, Georgiev GP (2004). "Interaction of the S100A4 (Mts1) protein with septins Sept2, Sept6, and Sept7 in vitro.". Dokl. Biochem. Biophys. 391: 195–7. doi:10.1023/A:1025149005902. PMID 14531065.
- She YM, Huang YW, Zhang L, Trimble WS (2004). "Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo.". Rapid Commun. Mass Spectrom. 18 (10): 1123–30. doi:10.1002/rcm.1453. PMID 15150837.
- Nagata K, Asano T, Nozawa Y, Inagaki M (2005). "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11.". J. Biol. Chem. 279 (53): 55895–904. doi:10.1074/jbc.M406153200. PMID 15485874.
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
- Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Spiliotis ET, Kinoshita M, Nelson WJ (2005). "A mitotic septin scaffold required for Mammalian chromosome congression and segregation.". Science 307 (5716): 1781–5. doi:10.1126/science.1106823. PMC 3368603. PMID 15774761.
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