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Volumn 412, Issue 1, 2011, Pages 3-13

The molecular basis of the Caskin1 and Mint1 interaction with CASK

Author keywords

calmodulin kinase; peptide motif; peptide protein interaction; scaffolding protein; TIAM1

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE I; MINT1 PROTEIN; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 84860390102     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.07.005     Document Type: Article
Times cited : (36)

References (50)
  • 1
    • 33745739734 scopus 로고    scopus 로고
    • The role of the MAGUK protein CASK in neural development and synaptic function
    • Hsueh Y.P. The role of the MAGUK protein CASK in neural development and synaptic function Curr. Med. Chem. 13 2006 1915 1927
    • (2006) Curr. Med. Chem. , vol.13 , pp. 1915-1927
    • Hsueh, Y.P.1
  • 2
    • 0029914941 scopus 로고    scopus 로고
    • CASK: A novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata Y., Butz S., and Südhof T.C. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins J. Neurosci. 16 1996 2488 2494 (Pubitemid 26124345)
    • (1996) Journal of Neuroscience , vol.16 , Issue.8 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Sudhof, T.C.3
  • 3
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins R., Hajnal A.F., Harp S.A., and Kim S.K. The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins Development 122 1996 97 111 (Pubitemid 26038422)
    • (1996) Development , vol.122 , Issue.1 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 5
    • 0034673760 scopus 로고    scopus 로고
    • Nuclear translocation and transcription regulation by the membrane- associated guanylate kinase CASK/LIN-2
    • DOI 10.1038/35005118
    • Hsueh Y.P., Wang T.F., Yang F.C., and Sheng M. Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2 Nature 404 2000 298 302 (Pubitemid 30163549)
    • (2000) Nature , vol.404 , Issue.6775 , pp. 298-302
    • Hsueh, Y.-P.1    Wang, T.-F.2    Yang, F.-C.3    Sheng, M.4
  • 6
    • 70449371457 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent serine protein kinase and mental retardation
    • Hsueh Y.P. Calcium/calmodulin-dependent serine protein kinase and mental retardation Ann. Neurol. 66 2009 438 443
    • (2009) Ann. Neurol. , vol.66 , pp. 438-443
    • Hsueh, Y.P.1
  • 7
    • 49449117177 scopus 로고    scopus 로고
    • The CASK gene harbored in a deletion detected by array-CGH as a potential candidate for a gene causative of X-linked dominant mental retardation
    • Hayashi S., Mizuno S., Migita O., Okuyama T., Makita Y., and Hata A. The CASK gene harbored in a deletion detected by array-CGH as a potential candidate for a gene causative of X-linked dominant mental retardation Am. J. Med. Genet., Part A 146A 2008 2145 2151
    • (2008) Am. J. Med. Genet., Part A , vol.146 A , pp. 2145-2151
    • Hayashi, S.1    Mizuno, S.2    Migita, O.3    Okuyama, T.4    Makita, Y.5    Hata, A.6
  • 8
    • 50449089620 scopus 로고    scopus 로고
    • Mutations of CASK cause an X-linked brain malformation phenotype with microcephaly and hypoplasia of the brainstem and cerebellum
    • Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., and Sudi J. Mutations of CASK cause an X-linked brain malformation phenotype with microcephaly and hypoplasia of the brainstem and cerebellum Nat. Genet. 40 2008 1065 1067
    • (2008) Nat. Genet. , vol.40 , pp. 1065-1067
    • Najm, J.1    Horn, D.2    Wimplinger, I.3    Golden, J.A.4    Chizhikov, V.V.5    Sudi, J.6
  • 9
    • 66749148353 scopus 로고    scopus 로고
    • A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation
    • Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., and Hardy C. A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation Nat. Genet. 41 2009 535 543
    • (2009) Nat. Genet. , vol.41 , pp. 535-543
    • Tarpey, P.S.1    Smith, R.2    Pleasance, E.3    Whibley, A.4    Edkins, S.5    Hardy, C.6
  • 10
    • 65449135942 scopus 로고    scopus 로고
    • An X-linked microcephaly syndrome caused by disruptions of CASK implicates the CASK-TBR1-RELN pathway in human brain development
    • Bailey K.A., and Aldinger K.A. An X-linked microcephaly syndrome caused by disruptions of CASK implicates the CASK-TBR1-RELN pathway in human brain development Clin. Genet. 75 2009 424 425
    • (2009) Clin. Genet. , vol.75 , pp. 424-425
    • Bailey, K.A.1    Aldinger, K.A.2
  • 11
    • 77951622870 scopus 로고    scopus 로고
    • CASK mutations are frequent in males and cause X-linked nystagmus and variable XLMR phenotypes
    • Hackett A., Tarpey P.S., Licata A., Cox J., Whibley A., and Boyle J. CASK mutations are frequent in males and cause X-linked nystagmus and variable XLMR phenotypes Eur. J. Hum. Genet. 18 2010 544 552
    • (2010) Eur. J. Hum. Genet. , vol.18 , pp. 544-552
    • Hackett, A.1    Tarpey, P.S.2    Licata, A.3    Cox, J.4    Whibley, A.5    Boyle, J.6
  • 13
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • DOI 10.1016/S0092-8674(00)81736-5
    • Butz S., Okamoto M., and Südhof T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain Cell 94 1998 773 782 (Pubitemid 28436009)
    • (1998) Cell , vol.94 , Issue.6 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 15
    • 0036617907 scopus 로고    scopus 로고
    • CASK participates in alternative tripartite complexes in which Mint 1 competes for binding with caskin 1, a novel CASK-binding protein
    • Tabuchi K., Biederer T., Butz S., and Sudhof T.C. CASK participates in alternative tripartite complexes in which Mint 1 competes for binding with caskin 1, a novel CASK-binding protein J. Neurosci. 22 2002 4264
    • (2002) J. Neurosci. , vol.22 , pp. 4264
    • Tabuchi, K.1    Biederer, T.2    Butz, S.3    Sudhof, T.C.4
  • 17
    • 0037040232 scopus 로고    scopus 로고
    • Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains
    • DOI 10.1074/jbc.M110792200
    • Li Y., Spangenberg O., Paarmann I., Konrad M., and Lavie A. Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains J. Biol. Chem. 277 2002 4159 4165 (Pubitemid 34968677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 4159-4165
    • Li, Y.1    Spangenberg, O.2    Paarmann, I.3    Konrad, M.4    Lavie, A.5
  • 18
    • 0037382349 scopus 로고    scopus 로고
    • CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase
    • Yap C.C., Liang F., Yamazaki Y., Muto Y., Kishida H., and Hayashida T. CIP98, a novel PDZ domain protein, is expressed in the central nervous system and interacts with calmodulin-dependent serine kinase J. Neurochem. 85 2003 123 134 (Pubitemid 36389702)
    • (2003) Journal of Neurochemistry , vol.85 , Issue.1 , pp. 123-134
    • Yap, C.C.1    Liang, F.2    Yamazaki, Y.3    Muto, Y.4    Kishida, H.5    Hayashida, T.6    Hashikawa, T.7    Yano, R.8
  • 19
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • DOI 10.1083/jcb.142.1.139
    • Hsueh Y.P., Yang F.C., Kharazia V., Naisbitt S., Cohen A.R., Weinberg R.J., and Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses J. Cell Biol. 142 1998 139 151 (Pubitemid 28341146)
    • (1998) Journal of Cell Biology , vol.142 , Issue.1 , pp. 139-151
    • Hsueh, Y.-P.1    Yang, F.-C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 21
    • 0037016687 scopus 로고    scopus 로고
    • Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain
    • DOI 10.1074/jbc.M109806200
    • Fallon L., Moreau F., Croft B.G., Labib N., Gu W.J., and Fon E.A. 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 2002 486 491 (Pubitemid 34952083)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 486-491
    • Fallon, L.1    Moreau, F.2    Croft, B.G.3    Labib, N.4    Gu, W.-J.5    Fon, E.A.6
  • 22
    • 0037200037 scopus 로고    scopus 로고
    • SynCAM, a synaptic adhesion molecule that drives synapse assembly
    • DOI 10.1126/science.1072356
    • Biederer T., Sara Y., Mozhayeva M., Atasoy D., Liu X., Kavalali E.T., and Südhof T.C. SynCAM, a synaptic adhesion molecule that drives synapse assembly Science 297 2002 1525 1531 (Pubitemid 34970994)
    • (2002) Science , vol.297 , Issue.5586 , pp. 1525-1531
    • Biederer, T.1    Sara, Y.2    Mozhayeva, M.3    Atasoy, D.4    Liu, X.5    Kavalali, E.T.6    Sudhof, T.C.7
  • 25
    • 33947256308 scopus 로고    scopus 로고
    • Docking interactions in protein kinase and phosphatase networks
    • DOI 10.1016/j.sbi.2006.10.008, PII S0959440X06001801, Catalysis and Regulation / Proteins
    • Reményi A., Good M.C., and Lim W.A. Docking interactions in protein kinase and phosphatase networks Curr. Opin. Struct. Biol. 16 2006 676 685 (Pubitemid 44827730)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.6 , pp. 676-685
    • Remenyi, A.1    Good, M.C.2    Lim, W.A.3
  • 27
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: Recent updates and new developments
    • Letunic I., Doerks T., and Bork P. SMART 6: recent updates and new developments Nucleic Acids Res. 37 2009 D229 D232
    • (2009) Nucleic Acids Res. , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 31
    • 0030665808 scopus 로고    scopus 로고
    • Green fluorescent protein as a signal for protein-protein interactions
    • Park S.H., and Raines R.T. Green fluorescent protein as a signal for protein-protein interactions Protein Sci. 6 1997 2344 2349 (Pubitemid 27490744)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2344-2349
    • Park, S.-H.1    Raines, R.T.2
  • 32
    • 3242687294 scopus 로고    scopus 로고
    • Fluorescence gel retardation assay to detect protein-protein interactions
    • Park S.H., and Raines R.T. Fluorescence gel retardation assay to detect protein-protein interactions Methods Mol. Biol. 261 2004 155 160
    • (2004) Methods Mol. Biol. , vol.261 , pp. 155-160
    • Park, S.H.1    Raines, R.T.2
  • 36
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H., Erez E., Martz E., Pupko T., and Ben-Tal N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 2010 W529 W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 37
    • 77953573815 scopus 로고    scopus 로고
    • Sub-angstrom modeling of complexes between flexible peptides and globular proteins
    • Raveh B., London N., and Schueler-Furman O. Sub-angstrom modeling of complexes between flexible peptides and globular proteins Proteins 78 2010 2029 2040
    • (2010) Proteins , vol.78 , pp. 2029-2040
    • Raveh, B.1    London, N.2    Schueler-Furman, O.3
  • 38
    • 75849126506 scopus 로고    scopus 로고
    • The structural basis of peptide-protein binding strategies
    • London N., Movshovitz-Attias D., and Schueler-Furman O. The structural basis of peptide-protein binding strategies Structure 18 2010 188 199
    • (2010) Structure , vol.18 , pp. 188-199
    • London, N.1    Movshovitz-Attias, D.2    Schueler-Furman, O.3
  • 39
    • 49549122501 scopus 로고    scopus 로고
    • Understanding eukaryotic linear motifs and their role in cell signaling and regulation
    • Diella F., Haslam N., Chica C., Budd A., Michael S., and Brown N.P. Understanding eukaryotic linear motifs and their role in cell signaling and regulation Front. Biosci. 13 2008 6580 6603
    • (2008) Front. Biosci. , vol.13 , pp. 6580-6603
    • Diella, F.1    Haslam, N.2    Chica, C.3    Budd, A.4    Michael, S.5    Brown, N.P.6
  • 40
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: Evolutionary interaction switches
    • DOI 10.1016/j.febslet.2005.04.005, PII S0014579305004618
    • Neduva V., and Russell R.B. Linear motifs: evolutionary interaction switches FEBS Lett. 579 2005 3342 3345 (Pubitemid 40804684)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 41
    • 0028225439 scopus 로고
    • Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins
    • DOI 10.1016/0092-8674(94)90216-X
    • Habets G.G., Scholtes E.H., Zuydgeest D., van der Kammen R.A., Stam J.C., Berns A., and Collard J.G. Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins Cell 77 1994 537 549 (Pubitemid 24153994)
    • (1994) Cell , vol.77 , Issue.4 , pp. 537-549
    • Habets, G.G.M.1    Scholtes, E.H.M.2    Zuydgeest, D.3    Van Der Kammen, R.A.4    Stam, J.C.5    Berns, A.6    Collard, J.G.7
  • 42
    • 1642343506 scopus 로고    scopus 로고
    • The role of the guanine nucleotide exchange factor Tiam1 in cellular migration, invasion, adhesion and tumor progression
    • DOI 10.1023/B:BREA.0000018421.31632.e6
    • Minard M.E., Kim L.S., Price J.E., and Gallick G.E. The role of the guanine nucleotide exchange factor Tiam1 in cellular migration, invasion, adhesion and tumor progression Breast Cancer Res. Treat. 84 2004 21 32 (Pubitemid 38388857)
    • (2004) Breast Cancer Research and Treatment , vol.84 , Issue.1 , pp. 21-32
    • Minard, M.E.1    Kim, L.-S.2    Price, J.E.3    Gallick, G.E.4
  • 43
    • 0036369804 scopus 로고    scopus 로고
    • Genetic studies define MAGUK proteins as regulators of epithelial cell polarity
    • Caruana G. Genetic studies define MAGUK proteins as regulators of epithelial cell polarity Int. J. Dev. Biol. 46 2002 511 518 (Pubitemid 36841019)
    • (2002) International Journal of Developmental Biology , vol.46 , pp. 511-518
    • Caruana, G.1
  • 44
    • 33744999597 scopus 로고    scopus 로고
    • Tiam1 takes PARt in cell polarity
    • DOI 10.1016/j.tcb.2006.04.001, PII S0962892406000985
    • Mertens A.E.E., Pegtel D.M., and Collard J.G. Tiam1 takes PARt in cell polarity Trends Cell Biol. 16 2006 308 316 (Pubitemid 43868087)
    • (2006) Trends in Cell Biology , vol.16 , Issue.6 , pp. 308-316
    • Mertens, A.E.E.1    Pegtel, D.M.2    Collard, J.G.3
  • 45
    • 0030948849 scopus 로고    scopus 로고
    • Expression of Tiam-1 in the developing brain suggests a role for the Tiam-1-Rac signaling pathway in cell migration and neurite outgrowth
    • DOI 10.1006/mcne.1997.0602
    • Ehler E., van Leeuwen F., Collard J.G., and Salinas P.C. Expression of Tiam-1 in the developing brain suggests a role for the Tiam-1-Rac signaling pathway in cell migration and neurite outgrowth Mol. Cell. Neurosci. 9 1997 1 12 (Pubitemid 27240923)
    • (1997) Molecular and Cellular Neurosciences , vol.9 , Issue.1 , pp. 1-12
    • Ehler, E.1    Van Leeuwen, F.2    Collard, J.G.3    Salinas, P.C.4
  • 46
    • 0042967835 scopus 로고    scopus 로고
    • The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal migration
    • DOI 10.1093/emboj/cdg413
    • Kawauchi T., Chihama K., Yo-ichi N., and Hoshino M. The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal migration EMBO J. 22 2003 4190 4201 (Pubitemid 37021747)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4190-4201
    • Kawauchi, T.1    Chihama, K.2    Nabeshima, Y.-I.3    Hoshino, M.4
  • 47
    • 47549102433 scopus 로고    scopus 로고
    • SUMOylation of the MAGUK protein CASK regulates dendritic spinogenesis
    • Chao H.W., Hong C.J., Huang T.N., Lin Y.L., and Hsueh Y.P. SUMOylation of the MAGUK protein CASK regulates dendritic spinogenesis J. Cell Biol. 182 2008 141 155
    • (2008) J. Cell Biol. , vol.182 , pp. 141-155
    • Chao, H.W.1    Hong, C.J.2    Huang, T.N.3    Lin, Y.L.4    Hsueh, Y.P.5
  • 48
    • 33644747349 scopus 로고    scopus 로고
    • The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis
    • DOI 10.1038/ncb1368, PII N1368
    • Zhang H., and Macara I.G. The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis Nat. Cell Biol. 8 2006 227 237 (Pubitemid 43336064)
    • (2006) Nature Cell Biology , vol.8 , Issue.3 , pp. 227-237
    • Zhang, H.1    Macara, I.G.2
  • 50
    • 0029904173 scopus 로고    scopus 로고
    • Screening of peptide libraries linked to lac repressor
    • DOI 10.1016/S0076-6879(96)67012-8
    • Schatz P.J., Cull M.G., Martin E.L., and Gates C.M. Screening of peptide libraries linked to lac repressor Methods Enzymol. 267 1996 171 191 (Pubitemid 26159222)
    • (1996) Methods in Enzymology , vol.267 , pp. 171-191
    • Schatz, P.J.1    Cull, M.G.2    Martin, E.L.3    Gates, C.M.4


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