CASK

From Wikipedia, the free encyclopedia

Calcium/calmodulin-dependent serine protein kinase (MAGUK family)

PDB rendering based on 1kgd.

Available structures: 1kgd, 1kwa, 1rso, 1y74, 1zl8

Identifiers

Symbol(s)

CASK; LIN2

External IDs

OMIM: 300172 MGI: 1309489 HomoloGene: 2736

Gene ontology
Molecular Function:	• nucleotide binding • guanylate kinase activity • protein serine/threonine kinase activity • protein binding • calmodulin binding • ATP binding • kinase activity • transferase activity
Cellular Component:	• cytosol • plasma membrane • actin cytoskeleton • basolateral plasma membrane • synaptosome • synapse
Biological Process:	• protein amino acid phosphorylation • cell adhesion • positive regulation of transcription from RNA polymerase II promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003688 (mRNA)
NP_003679 (protein)

NM_009806 (mRNA)
NP_033936 (protein)

Location

Chr X: 41.26 - 41.67 Mb

Chr X: 12.68 - 13 Mb

Pubmed search

[1]

[2]

Calcium/calmodulin-dependent serine protein kinase (MAGUK family), also known as CASK, is a human gene.^[1]

[edit] References

^ Entrez Gene: CASK Calcium/calmodulin-dependent serine protein kinase (MAGUK family).

[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): 317–25. 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): 129–38. PMID 9660868.
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): 139–51. PMID 9660869.
Dimitratos SD, Stathakis DG, Nelson CA, et al. (1998). "The location of human CASK at Xp11.4 identifies this gene as a candidate for X-linked optic atrophy.". Genomics 51 (2): 308–9. doi:10.1006/geno.1998.5404. PMID 9722958.
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): 773–82. 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): 31633–6. 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): 24453–6. 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): 41192–200. 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): 934–7. PMID 11003712.
Biederer T, Südhof TC (2001). "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 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): 9291–6. 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. 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): 486–91. 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.