Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASKgene.[5][6] 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.
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[]
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 neurexins and syndecans.
Clinical importance[]
This gene has been implicated in X-linked mental retardation,[7] including specifically mental retardation and microcephaly with pontine and cerebellar hypoplasia.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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. PMID9722958.
^Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z, Luo X (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. PMID15694377.
Zhu ZQ, Wang D, Xiang D, Yuan YX, 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. PMID24140090.
Wang Y, Li R, Du D, Zhang C, Yuan H, Zeng R, Chen Z (2006). "Proteomic analysis reveals novel molecules involved in insulin signaling pathway". J. Proteome Res. 5 (4): 846–55. CiteSeerX10.1.1.583.5128. doi:10.1021/pr050391m. PMID16602692.
Wei JL, Fu ZX, Fang M, Zhou QY, Zhao QN, Guo JB, Lu WD, Wang H (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. PMID24927672.
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. PMID9546224.
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. PMID10749215.
Stevenson D, Laverty HG, Wenwieser S, Douglas M, Wilson JB (October 2000). "Mapping and expression analysis of the human CASK gene". Mamm. Genome. 11 (10): 934–7. doi:10.1007/s003350010170. PMID11003712.
Olsen O, Liu H, Wade JB, Merot J, Welling PA (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. PMID11742811.
External links[]
Human CASK genome location and CASK gene details page in the UCSC Genome Browser.
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PDB gallery
1kgd: Crystal Structure of the Guanylate Kinase-like Domain of Human CASK
1kwa: HUMAN CASK/LIN-2 PDZ DOMAIN
1rso: Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms of supra-molecular assemblies
1y74: Solution Structure of mLin-2/mLin-7 L27 Domain Complex
1zl8: NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins