메뉴 건너뛰기




Volumn 83, Issue 4, 2002, Pages 1013-1017

ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53

Author keywords

Insulin; IRSp53; Postsynaptic density; ProSAP; Shank; Synapse

Indexed keywords

CELL PROTEIN; COMPLEMENTARY DNA; GLUTAMATE RECEPTOR; GUANOSINE TRIPHOSPHATASE; INSULIN RECEPTOR; N METHYL DEXTRO ASPARTIC ACID; PROTEIN IRSP53; PROTEIN PROSAP; PROTEIN SHANK; PROTEIN TYROSINE KINASE; RHO FACTOR; UNCLASSIFIED DRUG;

EID: 0036846301     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2002.01204.x     Document Type: Article
Times cited : (113)

References (25)
  • 1
    • 0033197996 scopus 로고    scopus 로고
    • The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses
    • Abbott M. A., Wells D. G. and Fallon J. R. (1999) The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses. J. Neurosci. 19, 7300-7308.
    • (1999) J. Neurosci. , vol.19 , pp. 7300-7308
    • Abbott, M.A.1    Wells, D.G.2    Fallon, J.R.3
  • 3
    • 0035955643 scopus 로고    scopus 로고
    • Synaptic scaffolding proteins in rat brain ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin
    • Bockers T. M., Mameza M. G., Kreutz M. R., Bockmann J., Weise C., Buck F., Richter D., Gundelfinger E. D. and Kreienkamp H. J. (2001) Synaptic scaffolding proteins in rat brain ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin. J. Biol. Chem. 276, 40104-40112.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40104-40112
    • Bockers, T.M.1    Mameza, M.G.2    Kreutz, M.R.3    Bockmann, J.4    Weise, C.5    Buck, F.6    Richter, D.7    Gundelfinger, E.D.8    Kreienkamp, H.J.9
  • 6
    • 0036316727 scopus 로고    scopus 로고
    • ProSAP/Shank proteins - A family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease
    • Boeckers T. M., Bockmann J., Kreutz M. R. and Gundelfinger E. D. (2002) ProSAP/Shank proteins - A family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease. J. Neurochem. 81, 903-910.
    • (2002) J. Neurochem. , vol.81 , pp. 903-910
    • Boeckers, T.M.1    Bockmann, J.2    Kreutz, M.R.3    Gundelfinger, E.D.4
  • 8
    • 0031656074 scopus 로고    scopus 로고
    • Identification of a novel cortactin SH3 domain-binding protein and its localization to growth cones of cultured neurons
    • Du Y., Weed S. A., Xiong W. C., Marshall T. D. and Parsons J. T. (1998) Identification of a novel cortactin SH3 domain-binding protein and its localization to growth cones of cultured neurons. Mol. Cell Biol. 18, 5838-5851.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5838-5851
    • Du, Y.1    Weed, S.A.2    Xiong, W.C.3    Marshall, T.D.4    Parsons, J.T.5
  • 9
    • 0018090354 scopus 로고
    • Insulin receptors are widely distributed in the central nervous system of the rat
    • Havrankova J., Roth J. and Brownstein M. (1978) Insulin receptors are widely distributed in the central nervous system of the rat. Nature 27, 827-829.
    • (1978) Nature , vol.27 , pp. 827-829
    • Havrankova, J.1    Roth, J.2    Brownstein, M.3
  • 10
    • 0035654078 scopus 로고    scopus 로고
    • Dendritic spines: Structure dynamics and regulation
    • Hering H. and Sheng M. (2001) Dendritic spines: Structure dynamics and regulation. Nat. Rev. Neurosci. 2, 2880-2888.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 2880-2888
    • Hering, H.1    Sheng, M.2
  • 11
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B. K., Williamson M. P. and Sudol M. (2000) The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 13
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S. and Takenawa T. (2000) IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 7, 732-735.
    • (2000) Nature , vol.7 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 14
    • 0033165926 scopus 로고    scopus 로고
    • Shank a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S., Kim E., Tu J. C., Xiao B., Sala C., Valtschanoff J., Weinberg R. J., Worley P. F. and Sheng M. (1999) Shank a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23, 569-582.
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1    Kim, E.2    Tu, J.C.3    Xiao, B.4    Sala, C.5    Valtschanoff, J.6    Weinberg, R.J.7    Worley, P.F.8    Sheng, M.9
  • 15
    • 0032891376 scopus 로고    scopus 로고
    • Identification of BAIAP2 (BAI-associated protein 2) a novel human homologue of hamster IRSp53 whose SH3 domain interacts with the cytoplasmic domain of BAII
    • Oda K., Shiratsuchi T., Nishimori H., Inazawa J., Yoshikawa H., Taketani Y., Nakamura Y. and Tokino T. (1999) Identification of BAIAP2 (BAI-associated protein 2) a novel human homologue of hamster IRSp53 whose SH3 domain interacts with the cytoplasmic domain of BAII. Cytogenet. Cell. Genet. 84, 75-82.
    • (1999) Cytogenet. Cell. Genet. , vol.84 , pp. 75-82
    • Oda, K.1    Shiratsuchi, T.2    Nishimori, H.3    Inazawa, J.4    Yoshikawa, H.5    Taketani, Y.6    Nakamura, Y.7    Tokino, T.8
  • 16
    • 0035930579 scopus 로고    scopus 로고
    • Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton
    • Okamoto P. M., Gamby C., Wells D., Fallon J. and Vallee R. B. (2001) Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton. J. Biol. Chem. 21, 48458-48465.
    • (2001) J. Biol. Chem. , vol.21 , pp. 48458-48465
    • Okamoto, P.M.1    Gamby, C.2    Wells, D.3    Fallon, J.4    Vallee, R.B.5
  • 17
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • Sala C., Piech V., Wilson N. R., Passafaro M., Liu G. and Sheng M. (2001) Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 31, 115-130.
    • (2001) Neuron , vol.31 , pp. 115-130
    • Sala, C.1    Piech, V.2    Wilson, N.R.3    Passafaro, M.4    Liu, G.5    Sheng, M.6
  • 18
    • 0030583645 scopus 로고    scopus 로고
    • Preproinsulin I and II mRNAs and insulin electron microscopic immunoreaction are present within the rat fetal nervous system
    • Schechter R., Beju D., Gaffney T., Schaefer F. and Whetsell L. (1996) Preproinsulin I and II mRNAs and insulin electron microscopic immunoreaction are present within the rat fetal nervous system. Brain Res. 14, 16-27.
    • (1996) Brain Res. , vol.14 , pp. 16-27
    • Schechter, R.1    Beju, D.2    Gaffney, T.3    Schaefer, F.4    Whetsell, L.5
  • 19
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • Sheng M. and Kim E. (2000) The Shank family of scaffold proteins. J. Cell Sci. 113, 1851-1856.
    • (2000) J. Cell Sci. , vol.113 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 20
    • 0035853124 scopus 로고    scopus 로고
    • Insulin promotes rapid delivery of N-methyl-D-aspartate receptors to the cell surface by exocytosis
    • Skeberdis V. A., Lan J., Zheng X., Zukin R. S. and Bennett M. V. (2001) Insulin promotes rapid delivery of N-methyl-D-aspartate receptors to the cell surface by exocytosis. Proc. Natl Acad. Sci. USA 13, 3561-3566.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.13 , pp. 3561-3566
    • Skeberdis, V.A.1    Lan, J.2    Zheng, X.3    Zukin, R.S.4    Bennett, M.V.5
  • 22
    • 0025217801 scopus 로고
    • Release of immunoreactive insulin from rat brain synaptosomes under depolarizing conditions
    • Wei L. T., Matsumoto H. and Rhoads D. E. (1990) Release of immunoreactive insulin from rat brain synaptosomes under depolarizing conditions. J. Neurochem. 54, 1661-1665.
    • (1990) J. Neurochem. , vol.54 , pp. 1661-1665
    • Wei, L.T.1    Matsumoto, H.2    Rhoads, D.E.3
  • 23
    • 0030020789 scopus 로고    scopus 로고
    • Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase
    • Yeh T. C., Ogawa W., Danielsen A. G. and Roth R. A. (1996) Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase. J. Biol. Chem. 9, 2921-2928.
    • (1996) J. Biol. Chem. , vol.9 , pp. 2921-2928
    • Yeh, T.C.1    Ogawa, W.2    Danielsen, A.G.3    Roth, R.A.4
  • 24
    • 0035970107 scopus 로고    scopus 로고
    • Contribution of cytoskeleton to the internalization of AMPA receptors
    • Zhou Q., Xiao M. and Nicoll R. A. (2001) Contribution of cytoskeleton to the internalization of AMPA receptors. Proc. Natl Acad. Sci. USA 30, 1261-1266.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.30 , pp. 1261-1266
    • Zhou, Q.1    Xiao, M.2    Nicoll, R.A.3
  • 25
    • 0040435762 scopus 로고    scopus 로고
    • Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain
    • Zitzer H., Honck H. H., Bachner D., Richter D. and Kreienkamp H. J. (1999) Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain. J. Biol. Chem. 274, 32997-33001.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32997-33001
    • Zitzer, H.1    Honck, H.H.2    Bachner, D.3    Richter, D.4    Kreienkamp, H.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.