CASK
From Wikipedia, the free encyclopedia
Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene.[1][2] This gene is also known by several other names: CMG 2 (CAMGUK protein 2), calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2.
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[edit] Genomics
This gene is located on the short arm of the X chromosome (Xp11.4). It is 404,253 bases in length and lies on the Crick (minus) strand. The encoded protein has 926 amino acids with a predicted molecular weight of 105.123 kDa.
[edit] Molecular biology
This protein is a multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. It interacts with the transcription factor TBR1 and binds to several cell-surface proteins including amyloid precursor protein, neurexins and syndecans.
Unlike many protein kinases, it does not require a divalent cation such as magnesium for catalytic activity
According to one study, CASK forms protein complexes with CINAP and TBR1.[3]
[edit] Clinical importance
This gene has been implicated in X linked mental retardation.[4]
[edit] Interactions
CASK has been shown to interact with KCNJ4,[5][6] ID1,[7] F11 receptor,[8][9] SDC2,[10][11] Parkin (ligase),[12] LIN7A,[6][13] Nephrin,[14] DLG4,[15] RPH3A,[16] DLG1,[6][15][17] APBA1,[13][18] KCNJ12[5][6] and ATP2B4.[19]
[edit] References
- ^ Dimitratos SD, Stathakis DG, Nelson CA, Woods DF, Bryant PJ (Nov 1998). "The location of human CASK at Xp11.4 identifies this gene as a candidate for X-linked optic atrophy". Genomics 51 (2): 308–309. doi:10.1006/geno.1998.5404. PMID 9722958.
- ^ "Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8573.
- ^ Wang GS, Hong CJ, Yen TY, Huang HY, Ou Y, Huang TN, Jung WG, Kuo TY, Sheng M, Wang TF, Hsueh YP (April 2004). "Transcriptional modification by a CASK-interacting nucleosome assembly protein". Neuron 42 (1): 113–128. doi:10.1016/S0896-6273(04)00139-4. PMID 15066269. http://linkinghub.elsevier.com/retrieve/pii/S0896627304001394.
- ^ Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C, O'Meara S, Latimer C, Dicks E, Menzies A, Stephens P, Blow M, Greenman C, Xue Y, Tyler-Smith C, Thompson D, Gray K, Andrews J, Barthorpe S, Buck G, Cole J, Dunmore R, Jones D, Maddison M, Mironenko T, Turner R, Turrell K, Varian J, West S, Widaa S, Wray P, Teague J, Butler A, Jenkinson A, Jia M, Richardson D, Shepherd R, Wooster R, Tejada MI, Martinez F, Carvill G, Goliath R, de Brouwer AP, van Bokhoven H, Van Esch H, Chelly J, Raynaud M, Ropers HH, Abidi FE, Srivastava AK, Cox J, Luo Y, Mallya U, Moon J, Parnau J, Mohammed S, Tolmie JL, Shoubridge C, Corbett M, Gardner A, Haan E, Rujirabanjerd S, Shaw M, Vandeleur L, Fullston T, Easton DF, Boyle J, Partington M, Hackett A, Field M, Skinner C, Stevenson RE, Bobrow M, Turner G, Schwartz CE, Gecz J, Raymond FL, Futreal PA, Stratton MR.(2009) A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation. Nat. Genet.
- ^ a b Leonoudakis, Dmitri; Conti Lisa R, Anderson Scott, Radeke Carolyn M, McGuire Leah M M, Adams Marvin E, Froehner Stanley C, Yates John R, Vandenberg Carol A (May. 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. (United States) 279 (21): 22331–22346. doi:10.1074/jbc.M400285200. ISSN 0021-9258. PMID 15024025.
- ^ a b c d Leonoudakis, Dmitri; Conti Lisa R, Radeke Carolyn M, McGuire Leah M M, Vandenberg Carol A (Apr. 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. (United States) 279 (18): 19051–19063. doi:10.1074/jbc.M400284200. ISSN 0021-9258. PMID 14960569.
- ^ Qi, Jie; Su Yongyue, Sun Rongju, Zhang Fang, Luo Xiaofeng, Yang Zongcheng, Luo Xiangdong (Mar. 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. (United States) 328 (2): 517–521. doi:10.1016/j.bbrc.2005.01.014. ISSN 0006-291X. PMID 15694377.
- ^ Martinez-Estrada, O M; Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (Mar. 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". J. Biol. Chem. (United States) 276 (12): 9291–9296. doi:10.1074/jbc.M006991200. ISSN 0021-9258. PMID 11120739.
- ^ Ebnet, K; Schulz C U, Meyer Zu Brickwedde M K, Pendl G G, Vestweber D (Sep. 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". J. Biol. Chem. (UNITED STATES) 275 (36): 27979–88. doi:10.1074/jbc.M002363200. ISSN 0021-9258. PMID 10856295.
- ^ Maximov, Anton; Tang Tie Shan, Bezprozvanny Ilya (Feb. 2003). "Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons". Mol. Cell. Neurosci. (United States) 22 (2): 271–283. doi:10.1016/S1044-7431(02)00027-1. ISSN 1044-7431. PMID 12676536.
- ^ Cohen, A R; Woods D F, Marfatia S M, Walther Z, Chishti A H, Anderson J M, Wood D F (Jul. 1998). "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells". J. Cell Biol. (UNITED STATES) 142 (1): 129–138. doi:10.1083/jcb.142.1.129. ISSN 0021-9525. PMC 2133028. PMID 9660868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133028.
- ^ Fallon, Lara; Moreau France, Croft Benjamin G, Labib Noura, Gu Wen-Jie, Fon Edward A (Jan. 2002). "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain". J. Biol. Chem. (United States) 277 (1): 486–491. doi:10.1074/jbc.M109806200. ISSN 0021-9258. PMID 11679592.
- ^ a b Borg, J P; Straight S W, Kaech S M, de Taddéo-Borg M, Kroon D E, Karnak D, Turner R S, Kim S K, Margolis B (Nov. 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. (UNITED STATES) 273 (48): 31633–31636. doi:10.1074/jbc.273.48.31633. ISSN 0021-9258. PMID 9822620.
- ^ Lehtonen, Sanna; Lehtonen Eero, Kudlicka Krystyna, Holthöfer Harry, Farquhar Marilyn G (Sep. 2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin". Am. J. Pathol. (United States) 165 (3): 923–936. doi:10.1016/S0002-9440(10)63354-8. ISSN 0002-9440. PMC 1618613. PMID 15331416. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1618613.
- ^ a b Chetkovich, Dane M; Bunn Robert C, Kuo Sheng-Han, Kawasaki Yoshimi, Kohwi Minoree, Bredt David S (Aug. 2002). "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms". J. Neurosci. (United States) 22 (15): 6415–25. PMID 12151521.
- ^ Zhang, Y; Luan Z, Liu A, Hu G (May. 2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. (Netherlands) 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. ISSN 0014-5793. PMID 11377421.
- ^ Nix, S L; Chishti A H, Anderson J M, Walther Z (Dec. 2000). "hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions". J. Biol. Chem. (UNITED STATES) 275 (52): 41192–41200. doi:10.1074/jbc.M002078200. ISSN 0021-9258. PMID 10993877.
- ^ Borg, J P; Lõpez-Figueroa M O, de Taddèo-Borg M, Kroon D E, Turner R S, Watson S J, Margolis B (Feb. 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. (UNITED STATES) 19 (4): 1307–16. ISSN 0270-6474. PMID 9952408.
- ^ Schuh, Kai; Uldrijan Stjepan, Gambaryan Stepan, Roethlein Nicola, Neyses Ludwig (Mar. 2003). "Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK". J. Biol. Chem. (United States) 278 (11): 9778–9783. doi:10.1074/jbc.M212507200. ISSN 0021-9258. PMID 12511555.
[edit] Further reading
- Hata Y, Butz S, Südhof TC (1996). "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins". J. Neurosci. 16 (8): 2488–94. PMID 8786425.
- Daniels DL, Cohen AR, Anderson JM, Brünger AT (1998). "Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition". Nat. Struct. Biol. 5 (4): 317–325. doi:10.1038/nsb0498-317. PMID 9546224.
- Cohen AR, Woods DF, Marfatia SM et al (1998). "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells". J. Cell Biol. 142 (1): 129–138. doi:10.1083/jcb.142.1.129. PMC 2133028. PMID 9660868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133028.
- Hsueh YP, Yang FC, Kharazia V et al (1998). "Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses". J. Cell Biol. 142 (1): 139–151. doi:10.1083/jcb.142.1.139. PMC 2133027. PMID 9660869. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133027.
- Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain". Cell 94 (6): 773–782. doi:10.1016/S0092-8674(00)81736-5. PMID 9753324.
- Borg JP, Straight SW, Kaech SM et al (1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–31636. doi:10.1074/jbc.273.48.31633. PMID 9822620.
- Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M et al (1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. PMID 9952408.
- Maximov A, Südhof TC, Bezprozvanny I (1999). "Association of neuronal calcium channels with modular adaptor proteins". J. Biol. Chem. 274 (35): 24453–24456. doi:10.1074/jbc.274.35.24453. PMID 10455105.
- Hsueh YP, Sheng M (1999). "Regulated expression and subcellular localization of syndecan heparan sulfate proteoglycans and the syndecan-binding protein CASK/LIN-2 during rat brain development". J. Neurosci. 19 (17): 7415–25. PMID 10460248.
- Hsueh YP, Wang TF, Yang FC, Sheng M (2000). "Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2". Nature 404 (6775): 298–302. doi:10.1038/35005118. PMID 10749215.
- Ebnet K, Schulz CU, Meyer Zu Brickwedde MK et al (2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". J. Biol. Chem. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
- Nix SL, Chishti AH, Anderson JM, Walther Z (2001). "hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions". J. Biol. Chem. 275 (52): 41192–41200. doi:10.1074/jbc.M002078200. PMID 10993877.
- Stevenson D, Laverty HG, Wenwieser S et al (2000). "Mapping and expression analysis of the human CASK gene". Mamm. Genome 11 (10): 934–937. doi:10.1007/s003350010170. PMID 11003712.
- Biederer T, Südhof TC (2001). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–39806. doi:10.1074/jbc.C000656200. PMID 11036064.
- Martinez-Estrada OM, Villa A, Breviario F et al (2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". J. Biol. Chem. 276 (12): 9291–9296. doi:10.1074/jbc.M006991200. PMID 11120739.
- Hsueh YP, Roberts AM, Volta M et al (2001). "Bipartite interaction between neurofibromatosis type I protein (neurofibromin) and syndecan transmembrane heparan sulfate proteoglycans". J. Neurosci. 21 (11): 3764–70. PMID 11356864.
- Zhang Y, Luan Z, Liu A, Hu G (2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. PMID 11377421.
- Fallon L, Moreau F, Croft BG et al (2002). "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain". J. Biol. Chem. 277 (1): 486–491. doi:10.1074/jbc.M109806200. PMID 11679592.
- Olsen O, Liu H, Wade JB et al (2002). "Basolateral membrane expression of the Kir 2.3 channel is coordinated by PDZ interaction with Lin-7/CASK complex". Am. J. Physiol., Cell Physiol. 282 (1): C183–95. doi:10.1152/ajpcell.00249.2001. PMID 11742811.
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