메뉴 건너뛰기




Volumn 22, Issue 11, 2002, Pages 4264-4273

CASK Participates in Alternative Tripartite Complexes in which Mint 1 Competes for Binding with Caskin 1, a Novel CASK-Binding Protein

Author keywords

CASK; Caskin; Lin 2; Mint 1; Neurexin; Scaffold; Synapse; Syndecan; Velis

Indexed keywords

ADAPTOR PROTEIN; ANKYRIN; BINDING PROTEIN; CASK PROTEIN; CASKIN 1; CASKIN 2; CELL SURFACE PROTEIN; ISOPROTEIN; NEUREXIN; PROTEIN MINT 1; UNCLASSIFIED DRUG; APBA1 PROTEIN, HUMAN; APBA1 PROTEIN, MOUSE; APBA1 PROTEIN, RAT; CALMODULIN DEPENDENT SERINE KINASE; CALMODULIN-DEPENDENT SERINE KINASE; CARRIER PROTEIN; CASKIN 1 PROTEIN, RAT; CASKIN 2 PROTEIN, RAT; CASKIN2 PROTEIN, HUMAN; CASKIN2 PROTEIN, MOUSE; HYBRID PROTEIN; MEMBRANE PROTEIN; NERVE PROTEIN; NUCLEOSIDE MONOPHOSPHATE KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN); RNA; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 0036617907     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.22-11-04264.2002     Document Type: Article
Times cited : (105)

References (31)
  • 1
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors: Direct binding to neurexins and recruitment of munc18
    • Biederer T, Südhof TC (2000) Mints as adaptors: direct binding to neurexins and recruitment of munc18. J Biol Chem 275:39803-39806.
    • (2000) J Biol Chem , vol.275 , pp. 39803-39806
    • Biederer, T.1    Südhof, T.C.2
  • 2
    • 0035930572 scopus 로고    scopus 로고
    • Cask and protein 4.1 support F-actin nucleation on neurexins
    • Biederer T, Südhof TC (2001) Cask and protein 4.1 support F-actin nucleation on neurexins. J Biol Chem 276:47869-47876.
    • (2001) J Biol Chem , vol.276 , pp. 47869-47876
    • Biederer, T.1    Südhof, T.C.2
  • 3
    • 0032510834 scopus 로고    scopus 로고
    • The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion
    • Borg JP, Yang Y, De Taddeo-Borg M, Margolis B, Turner RS (1998a) The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. J Biol Chem 273:14761-14766.
    • (1998) J Biol Chem , vol.273 , pp. 14761-14766
    • Borg, J.P.1    Yang, Y.2    De Taddeo-Borg, M.3    Margolis, B.4    Turner, R.S.5
  • 5
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • 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 94:773-782.
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Südhof, T.C.3
  • 6
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM, Wood DF (1998) Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J Cell Biol 142:129-138.
    • (1998) J Cell Biol , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3    Walther, Z.4    Chishti, A.H.5    Anderson, J.M.6    Wood, D.F.7
  • 7
    • 0030910976 scopus 로고    scopus 로고
    • Camguk, Lin-2, and CASK: Novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains
    • Dimitratos SD, Woods DF, Bryant PJ (1997) Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains. Mech Dev 63:127-130.
    • (1997) Mech Dev , vol.63 , pp. 127-130
    • Dimitratos, S.D.1    Woods, D.F.2    Bryant, P.J.3
  • 9
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE (1991) Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem 192:262-267.
    • (1991) Anal Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 10
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata Y, Slaughter CA, Südhof TC (1993) Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366: 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 11
    • 0029914941 scopus 로고    scopus 로고
    • CASK: A novel dlg/PSD95 homologue with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata Y, Butz S, Südhof TC (1996) CASK: a novel dlg/PSD95 homologue with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci 16:2488-2494.
    • (1996) J Neurosci , vol.16 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Südhof, T.C.3
  • 12
    • 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 AF, Harp SA, Kim SK (1996) The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development 122:97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 13
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • Hsueh YP, Yang C, Kharazia V, Naisbitt S, Cohen AR, Weinberg RJ, Sheng M (1998) Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. J Cell Biol 142:139-151.
    • (1998) J Cell Biol , vol.142 , pp. 139-151
    • Hsueh, Y.P.1    Yang, C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 14
    • 0034673760 scopus 로고    scopus 로고
    • Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
    • Hsueh YP, Wang TF, Yang FC, Sheng M (2000) Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature 404:298-302.
    • (2000) Nature , vol.404 , pp. 298-302
    • Hsueh, Y.P.1    Wang, T.F.2    Yang, F.C.3    Sheng, M.4
  • 15
    • 0032544565 scopus 로고    scopus 로고
    • The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
    • Kaech SM, Whitfield CW, Kim SK (1998) The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell 94:761-771.
    • (1998) Cell , vol.94 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 16
    • 0030720016 scopus 로고    scopus 로고
    • Polarized signaling: Basolateral receptor localization in epithelial cells by PDZ-containing proteins
    • Kim SK (1997) Polarized signaling: basolateral receptor localization in epithelial cells by PDZ-containing proteins. Curr Opin Cell Biol 9:853-859.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 853-859
    • Kim, S.K.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0032191192 scopus 로고    scopus 로고
    • Murine CASK is disrupted in a sex-linked cleft palate mouse mutant
    • Laverty HG, Wilson JB (1998) Murine CASK is disrupted in a sex-linked cleft palate mouse mutant. Genomics 53:29-41.
    • (1998) Genomics , vol.53 , pp. 29-41
    • Laverty, H.G.1    Wilson, J.B.2
  • 19
    • 0035937810 scopus 로고    scopus 로고
    • Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells
    • Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (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 276:9291-9296.
    • (2001) J Biol Chem , vol.276 , pp. 9291-9296
    • Martinez-Estrada, O.M.1    Villa, A.2    Breviario, F.3    Orsenigo, F.4    Dejana, E.5    Bazzoni, G.6
  • 20
    • 0040962408 scopus 로고    scopus 로고
    • Association of neuronal calcium channels with modular adaptor proteins
    • Maximov A, Sudhof TC, Bezprozvanny I (1999) Association of neuronal calcium channels with modular adaptor proteins. J Biol Chem 274:24453-24456.
    • (1999) J Biol Chem , vol.274 , pp. 24453-24456
    • Maximov, A.1    Sudhof, T.C.2    Bezprozvanny, I.3
  • 21
    • 0030592773 scopus 로고    scopus 로고
    • The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system
    • McLoughlin DM, Miller CC (1996) The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system. FEBS Lett 397:197-200.
    • (1996) FEBS Lett , vol.397 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.2
  • 22
    • 0034731375 scopus 로고    scopus 로고
    • hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions
    • Nix SL, Chishti AH, Anderson JM, Walther Z (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 275:41192-41200.
    • (2000) J Biol Chem , vol.275 , pp. 41192-41200
    • Nix, S.L.1    Chishti, A.H.2    Anderson, J.M.3    Walther, Z.4
  • 23
    • 0031465172 scopus 로고    scopus 로고
    • Mints, munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M, Südhof TC (1997) Mints, munc18-interacting proteins in synaptic vesicle exocytosis. J Biol Chem 272:31459-31464.
    • (1997) J Biol Chem , vol.272 , pp. 31459-31464
    • Okamoto, M.1    Südhof, T.C.2
  • 24
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson T, Nash P (2000) Protein-protein interactions define specificity in signal transduction. Genes Dev 14:1027-1047.
    • (2000) Genes Dev , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 25
    • 0032544612 scopus 로고    scopus 로고
    • LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia
    • Rongo C, Whitfield CW, Rodal A, Kim SK, Kaplan JM (1998) LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Cell 94:751-759.
    • (1998) Cell , vol.94 , pp. 751-759
    • Rongo, C.1    Whitfield, C.W.2    Rodal, A.3    Kim, S.K.4    Kaplan, J.M.5
  • 28
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou M, Nakagawa T, Seog DH, Hirokawa N (2000) Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 288:1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 29
    • 0034916230 scopus 로고    scopus 로고
    • Pdz domains and the organization of supramolecular complexes
    • Sheng M, Sala C (2001) Pdz domains and the organization of supramolecular complexes. Annu Rev Neurosci 24:1-29.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 31
    • 0033462127 scopus 로고    scopus 로고
    • The organization of INAD-signaling complexes by a multivalent PDZ domain protein in Drosophila photoreceptor cells ensures sensitivity and speed of signaling
    • Tsunoda S, Zuker CS (1999) The organization of INAD-signaling complexes by a multivalent PDZ domain protein in Drosophila photoreceptor cells ensures sensitivity and speed of signaling. Cell Calcium 26: 165-171.
    • (1999) Cell Calcium , vol.26 , pp. 165-171
    • Tsunoda, S.1    Zuker, C.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.