메뉴 건너뛰기




Volumn 585, Issue 1, 2011, Pages 58-64

Direct demonstration of NCAM cis-dimerization and inhibitory effect of palmitoylation using the BRET2 technique

Author keywords

Bioluminescence resonance energy transfer; cis interaction; Homophilic binding; Neural cell adhesion molecule; Palmitoylation

Indexed keywords

GREEN FLUORESCENT PROTEIN; NERVE CELL ADHESION MOLECULE;

EID: 78650867082     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.11.043     Document Type: Article
Times cited : (9)

References (32)
  • 1
    • 10844287931 scopus 로고    scopus 로고
    • Zippers make signals: NCAM-mediated molecular interactions and signal transduction
    • P.S. Walmod, K. Kolkova, V. Berezin, and E. Bock Zippers make signals: NCAM-mediated molecular interactions and signal transduction Neurochem. Res. 29 2004 2015 2035
    • (2004) Neurochem. Res. , vol.29 , pp. 2015-2035
    • Walmod, P.S.1    Kolkova, K.2    Berezin, V.3    Bock, E.4
  • 2
    • 77949877830 scopus 로고    scopus 로고
    • Signaling pathways involved in NCAM-induced neurite outgrowth
    • D.K. Ditlevsen, and K. Kolkova Signaling pathways involved in NCAM-induced neurite outgrowth Adv. Exp. Med. Biol. 663 2010 151 168
    • (2010) Adv. Exp. Med. Biol. , vol.663 , pp. 151-168
    • Ditlevsen, D.K.1    Kolkova, K.2
  • 3
    • 77949888723 scopus 로고    scopus 로고
    • NCAM in long-term potentiation and learning
    • B.P. Hartz, and L.C. Ronn NCAM in long-term potentiation and learning Adv. Exp. Med. Biol. 663 2010 257 270
    • (2010) Adv. Exp. Med. Biol. , vol.663 , pp. 257-270
    • Hartz, B.P.1    Ronn, L.C.2
  • 5
    • 77949905989 scopus 로고    scopus 로고
    • Extracellular protein interactions mediated by the neural cell adhesion molecule, NCAM: Heterophilic interactions between NCAM and cell adhesion molecules, extracellular matrix proteins, and viruses
    • J. Nielsen, N. Kulahin, and P.S. Walmod Extracellular protein interactions mediated by the neural cell adhesion molecule, NCAM: heterophilic interactions between NCAM and cell adhesion molecules, extracellular matrix proteins, and viruses Adv. Exp. Med. Biol. 663 2010 23 53
    • (2010) Adv. Exp. Med. Biol. , vol.663 , pp. 23-53
    • Nielsen, J.1    Kulahin, N.2    Walmod, P.S.3
  • 8
    • 77949892001 scopus 로고    scopus 로고
    • The neural cell adhesion molecule NCAM and lipid rafts
    • G.K. Povlsen, and D.K. Ditlevsen The neural cell adhesion molecule NCAM and lipid rafts Adv. Exp. Med. Biol. 663 2008 183 198
    • (2008) Adv. Exp. Med. Biol. , vol.663 , pp. 183-198
    • Povlsen, G.K.1    Ditlevsen, D.K.2
  • 9
    • 2342508857 scopus 로고    scopus 로고
    • Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion
    • V. Soroka Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion Structure 11 2003 1291 1301
    • (2003) Structure , vol.11 , pp. 1291-1301
    • Soroka, V.1
  • 10
    • 0023014152 scopus 로고
    • Differentiation state-dependent surface mobilities of two forms of the neural cell adhesion molecule
    • G.E. Pollerberg, M. Schachner, and J. Davoust Differentiation state-dependent surface mobilities of two forms of the neural cell adhesion molecule Nature 324 1986 462 465
    • (1986) Nature , vol.324 , pp. 462-465
    • Pollerberg, G.E.1    Schachner, M.2    Davoust, J.3
  • 11
    • 0023427237 scopus 로고
    • The 180-kD component of the neural cell adhesion molecule N-CAM is involved in a cell-cell contacts and cytoskeleton-membrane interactions
    • G.E. Pollerberg, K. Burridge, K.E. Krebs, S.R. Goodman, and M. Schachner The 180-kD component of the neural cell adhesion molecule N-CAM is involved in a cell-cell contacts and cytoskeleton-membrane interactions Cell Tissue Res. 250 1987 227 236
    • (1987) Cell Tissue Res. , vol.250 , pp. 227-236
    • Pollerberg, G.E.1    Burridge, K.2    Krebs, K.E.3    Goodman, S.R.4    Schachner, M.5
  • 14
    • 33847711498 scopus 로고    scopus 로고
    • GAP-43 regulates NCAM-180-mediated neurite outgrowth
    • I. Korshunova GAP-43 regulates NCAM-180-mediated neurite outgrowth J. Neurochem. 100 2007 1599 1612
    • (2007) J. Neurochem. , vol.100 , pp. 1599-1612
    • Korshunova, I.1
  • 15
    • 0032412614 scopus 로고    scopus 로고
    • Palmitoylation of the cytoplasmic domain of the neural cell adhesion molecule N-CAM serves as an anchor to cellular membranes
    • E.B. Little, G.M. Edelman, and B.A. Cunningham Palmitoylation of the cytoplasmic domain of the neural cell adhesion molecule N-CAM serves as an anchor to cellular membranes Cell Adhes. Commun. 6 1998 415 430
    • (1998) Cell Adhes. Commun. , vol.6 , pp. 415-430
    • Little, E.B.1    Edelman, G.M.2    Cunningham, B.A.3
  • 17
    • 0022345905 scopus 로고
    • Biosynthesis of the neural cell adhesion molecule: Characterization of polypeptide C
    • DOI 10.1083/jcb.101.6.2310
    • O. Nybroe, M. Albrechtsen, J. Dahlin, D. Linnemann, J.M. Lyles, C.J. Moller, and E. Bock Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C J. Cell Biol. 101 1985 2310 2315 (Pubitemid 16169962)
    • (1985) Journal of Cell Biology , vol.101 , Issue.6 , pp. 2310-2315
    • Nybroe, O.1    Albrechtsen, M.2    Dahlin, J.3
  • 18
    • 0038933866 scopus 로고    scopus 로고
    • Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinase activation during myelination
    • E.M. Kramer, C. Klein, T. Koch, M. Boytinck, and J. Trotter Compartmentation of Fyn kinase with glycosylphosphatidylinositol-anchored molecules in oligodendrocytes facilitates kinase activation during myelination J. Biol. Chem. 274 1999 29042 29049
    • (1999) J. Biol. Chem. , vol.274 , pp. 29042-29049
    • Kramer, E.M.1    Klein, C.2    Koch, T.3    Boytinck, M.4    Trotter, J.5
  • 19
    • 0036154848 scopus 로고    scopus 로고
    • Isolation and characterization of detergent-resistant microdomains responsive to NCAM-mediated signaling from growth cones
    • Q. He, and K.F. Meiri Isolation and characterization of detergent-resistant microdomains responsive to NCAM-mediated signaling from growth cones Mol. Cell. Neurosci. 19 2002 18 31
    • (2002) Mol. Cell. Neurosci. , vol.19 , pp. 18-31
    • He, Q.1    Meiri, K.F.2
  • 20
    • 0037193470 scopus 로고    scopus 로고
    • Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis
    • P. Niethammer, M. Delling, V. Sytnyk, A. Dityatev, K. Fukami, and M. Schachner Cosignaling of NCAM via lipid rafts and the FGF receptor is required for neuritogenesis J. Cell Biol. 157 2002 521 532
    • (2002) J. Cell Biol. , vol.157 , pp. 521-532
    • Niethammer, P.1    Delling, M.2    Sytnyk, V.3    Dityatev, A.4    Fukami, K.5    Schachner, M.6
  • 21
    • 0037598590 scopus 로고    scopus 로고
    • Neural cell adhesion molecule (NCAM) association with PKC2 via i spectrin is implicated in NCAM-mediated neurite outgrowth
    • I. Leshchyns'ka, V. Sytnyk, J.S. Morrow, and M. Schachner Neural cell adhesion molecule (NCAM) association with PKC2 via I spectrin is implicated in NCAM-mediated neurite outgrowth J. Cell Biol. 161 2003 625 639
    • (2003) J. Cell Biol. , vol.161 , pp. 625-639
    • Leshchyns'Ka, I.1    Sytnyk, V.2    Morrow, J.S.3    Schachner, M.4
  • 23
    • 0026750484 scopus 로고
    • Alternative splicing of the cytoplasmic domain of neural cell adhesion molecule alters its ability to act as a substrate for neurite outgrowth
    • P. Doherty, G. Rimon, D.A. Mann, and F.S. Walsh Alternative splicing of the cytoplasmic domain of neural cell adhesion molecule alters its ability to act as a substrate for neurite outgrowth J. Neurochem. 58 1992 2338 2341
    • (1992) J. Neurochem. , vol.58 , pp. 2338-2341
    • Doherty, P.1    Rimon, G.2    Mann, D.A.3    Walsh, F.S.4
  • 25
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of 1- and 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • J.F. Mercier, A. Salahpour, S. Angers, A. Breit, and M. Bouvier Quantitative assessment of 1- and 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer J. Biol. Chem. 277 2002 44925 44931
    • (2002) J. Biol. Chem. , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 26
    • 2542437470 scopus 로고    scopus 로고
    • Development of a BRET2 screening assay using -arrestin 2 mutants
    • M. Vrecl, R. Jorgensen, A. Pogacnik, and A. Heding Development of a BRET2 screening assay using -arrestin 2 mutants J. Biomol. Screen. 9 2004 322 333
    • (2004) J. Biomol. Screen. , vol.9 , pp. 322-333
    • Vrecl, M.1    Jorgensen, R.2    Pogacnik, A.3    Heding, A.4
  • 27
    • 37249040944 scopus 로고    scopus 로고
    • Phosphorylation of the 2-adrenergic receptor in plasma membranes by intrinsic GRK5
    • T.M. Tran, R. Jorgensen, and R.B. Clark Phosphorylation of the 2-adrenergic receptor in plasma membranes by intrinsic GRK5 Biochemistry 46 2007 14438 14449
    • (2007) Biochemistry , vol.46 , pp. 14438-14449
    • Tran, T.M.1    Jorgensen, R.2    Clark, R.B.3
  • 28
    • 0038374250 scopus 로고    scopus 로고
    • Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers
    • C. Couturier, and R. Jockers Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers J. Biol. Chem. 278 2003 26604 26611
    • (2003) J. Biol. Chem. , vol.278 , pp. 26604-26611
    • Couturier, C.1    Jockers, R.2
  • 29
    • 15744384803 scopus 로고    scopus 로고
    • Interaction of the insulin receptor with the receptor-like protein tyrosine phosphatases PTP and PTP in living cells
    • D. Lacasa, N. Boute, and T. Issad Interaction of the insulin receptor with the receptor-like protein tyrosine phosphatases PTP and PTP in living cells Mol. Pharmacol. 67 2005 1206 1213
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1206-1213
    • Lacasa, D.1    Boute, N.2    Issad, T.3
  • 31
    • 0030899695 scopus 로고    scopus 로고
    • The first immunoglobulin-like neural cell adhesion molecule (NCAM) domain is involved in double-reciprocal interaction with the second immunoglobulin-like NCAM domain and in heparin binding
    • V.V. Kiselyov, V. Berezin, T.E. Maar, V. Soroka, K. Edvardsen, A. Schousboe, and E. Bock The first immunoglobulin-like neural cell adhesion molecule (NCAM) domain is involved in double-reciprocal interaction with the second immunoglobulin-like NCAM domain and in heparin binding J. Biol. Chem. 272 1997 10125 10134
    • (1997) J. Biol. Chem. , vol.272 , pp. 10125-10134
    • Kiselyov, V.V.1    Berezin, V.2    Maar, T.E.3    Soroka, V.4    Edvardsen, K.5    Schousboe, A.6    Bock, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.