CASK

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Calcium/calmodulin-dependent serine protein kinase (MAGUK family)
Protein CASK PDB 1kgd.png
PDB rendering based on 1kgd.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CASK ; CAGH39; CAMGUK; CMG; FGS4; LIN2; MICPCH; MRXSNA; TNRC8
External IDs OMIM300172 MGI1309489 HomoloGene2736 GeneCards: CASK Gene
EC number 2.7.11.1
RNA expression pattern
PBB GE CASK 211208 s at tn.png
PBB GE CASK 207620 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8573 12361
Ensembl ENSG00000147044 ENSMUSG00000031012
UniProt O14936 O70589
RefSeq (mRNA) NM_001126054 NM_001284503
RefSeq (protein) NP_001119526 NP_001271432
Location (UCSC) Chr X:
41.37 – 41.78 Mb
Chr X:
13.52 – 13.85 Mb
PubMed search [1] [2]

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.

Gene[edit]

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 Daltons.

Function[edit]

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.

Clinical importance[edit]

This gene has been implicated in X-linked mental retardation,[3] including specifically mental retardation and microcephaly with pontine and cerebellar hypoplasia.[4]

Interactions[edit]

CASK has been shown to interact with:


References[edit]

  1. ^ Dimitratos S, Stathakis D, Nelson C, Woods D, Bryant P (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. 
  2. ^ "Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family)". 
  3. ^ Tarpey P, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C et al. (May 2009). "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation". Nat. Genet. 41 (5): 535–43. doi:10.1038/ng.367. PMC 2872007. PMID 19377476. 
  4. ^ Burglen L, Chantot-Bastaraud S, Garel C, Milh M, Touraine R, Zanni G et al. (2012). "Spectrum of pontocerebellar hypoplasia in 13 girls and boys with CASK mutations: confirmation of a recognizable phenotype and first description of a male mosaic patient". Orphanet Journal of Rare Diseases 7 (18): 18. doi:10.1186/1750-1172-7-18. PMC 3351739. PMID 22452838. 
  5. ^ a b Leonoudakis D, Conti L, Anderson S, Radeke C, McGuire L, Adams M et al. (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025. 
  6. ^ a b c d Leonoudakis D, Conti L, Radeke C, McGuire L, Vandenberg C (April 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. doi:10.1074/jbc.M400284200. PMID 14960569. 
  7. ^ a b Borg J, Straight S, Kaech S, de Taddéo-Borg M, Kroon D, Karnak D et al. (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620. 
  8. ^ Borg J, Lõpez-Figueroa M, de Taddèo-Borg M, Kroon D, Turner R, Watson S et al. (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. PMID 9952408. 
  9. ^ Schuh K, Uldrijan S, Gambaryan S, Roethlein N, Neyses L (March 2003). "Interaction of the plasma membrane Ca2+ pump 4b/CI with the Ca2+/calmodulin-dependent membrane-associated kinase CASK". J. Biol. Chem. 278 (11): 9778–83. doi:10.1074/jbc.M212507200. PMID 12511555. 
  10. ^ Wang G, Hong C, Yen T, Huang H, Ou Y, Huang T et al. (April 2004). "Transcriptional modification by a CASK-interacting nucleosome assembly protein". Neuron 42 (1): 113–28. doi:10.1016/S0896-6273(04)00139-4. PMID 15066269. 
  11. ^ a b Chetkovich D, Bunn R, Kuo S, Kawasaki Y, Kohwi M, Bredt D (August 2002). "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms". J. Neurosci. 22 (15): 6415–25. PMID 12151521. 
  12. ^ Nix S, Chishti A, Anderson J, Walther Z (December 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. 275 (52): 41192–200. doi:10.1074/jbc.M002078200. PMID 10993877. 
  13. ^ Martinez-Estrada O, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (March 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): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739. 
  14. ^ Ebnet K, Schulz C, Meyer Zu Brickwedde M, Pendl G, Vestweber D (September 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. 
  15. ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z et al. (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377. 
  16. ^ Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar M (September 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. 165 (3): 923–36. doi:10.1016/S0002-9440(10)63354-8. PMC 1618613. PMID 15331416. 
  17. ^ Fallon L, Moreau F, Croft B, Labib N, Gu W, Fon E (January 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): 486–91. doi:10.1074/jbc.M109806200. PMID 11679592. 
  18. ^ a b Zhang Y, Luan Z, Liu A, Hu G (May 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. 
  19. ^ Cohen A, Woods D, Marfatia S, Walther Z, Chishti A, Anderson J et al. (July 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): 129–38. doi:10.1083/jcb.142.1.129. PMC 2133028. PMID 9660868. 

Further reading[edit]

  • Zhu Z, Wang D, Xiang D, Yuan Y, Wang Y (2014). "Calcium/calmodulin-dependent serine protein kinase is involved in exendin-4-induced insulin secretion in INS-1 cells". Metab. Clin. Exp. 63 (1): 120–6. doi:10.1016/j.metabol.2013.09.009. PMID 24140090. 
  • Wang Y, Li R, Du D, Zhang C, Yuan H, Zeng R et al. (2006). "Proteomic analysis reveals novel molecules involved in insulin signaling pathway". J. Proteome Res. 5 (4): 846–55. doi:10.1021/pr050391m. PMID 16602692. 
  • Mukherjee K, Slawson J, Christmann B, Griffith L (2014). "Neuron-specific protein interactions of Drosophila CASK-β are revealed by mass spectrometry". Frontiers in Molecular Neuroscience 7. doi:10.3389/fnmol.2014.00058. PMC 4075472. PMID 25071438. 
  • Wei J, Fu Z, Fang M, Zhou Q, Zhao Q, Guo J et al. (2014). "High expression of CASK correlates with progression and poor prognosis of colorectal cancer". Tumour Biol. 35 (9): 9185–94. doi:10.1007/s13277-014-2179-3. PMID 24927672. 
  • Hata Y, Butz S, Südhof T (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 D, Cohen A, Anderson J, Brünger A (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. 
  • Hsueh Y, Yang F, Kharazia V, Naisbitt S, Cohen A, Weinberg R et al. (July 1998). "Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses". J. Cell Biol. 142 (1): 139–51. doi:10.1083/jcb.142.1.139. PMC 2133027. PMID 9660869. 
  • Butz S, Okamoto M, Südhof T (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 J, Straight S, Kaech S, de Taddéo-Borg M, Kroon D, Karnak D et al. (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620. 
  • Borg J, Lõpez-Figueroa M, de Taddèo-Borg M, Kroon D, Turner R, Watson S et al. (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. PMID 9952408. 
  • Maximov A, Südhof T, 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 Y, 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 Y, Wang T, Yang F, 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 C, Meyer Zu Brickwedde M, Pendl G, Vestweber D (September 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 S, Chishti A, Anderson J, 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 H, Wenwieser S, Douglas M, Wilson J (October 2000). "Mapping and expression analysis of the human CASK gene". Mamm. Genome 11 (10): 934–7. doi:10.1007/s003350010170. PMID 11003712. 
  • Biederer T, Südhof T (December 2000). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–6. doi:10.1074/jbc.C000656200. PMID 11036064. 
  • Martinez-Estrada O, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (March 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): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739. 
  • Hsueh Y, Roberts A, Volta M, Sheng M, Roberts R (June 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 (May 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 B, Labib N, Gu W, Fon E (January 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): 486–91. doi:10.1074/jbc.M109806200. PMID 11679592. 
  • Olsen O, Liu H, Wade J, Merot J, Welling P (January 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.