Literature DB >> 9232802

Interaction of ion channels and receptors with PDZ domain proteins.

H C Kornau1, P H Seeburg, M B Kennedy.   

Abstract

The complex anatomy of neurons demands a high degree of functional organization. Therefore, membrane receptors and ion channels are often localized to selected subcellular sites and coupled to specific signal transduction machineries. PDZ domains have come into focus as protein interaction modules that mediate the binding of a class of submembraneous proteins to membrane receptors and ion channels and thus subserve these organizational aspects. The structures of two PDZ domains have been resolved, which has led to a structural understanding of the specificity of interactions of various PDZ domains with their respective partners. The functional implications of PDZ domain interactions are now being addressed in vitro and in vivo.

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Year:  1997        PMID: 9232802     DOI: 10.1016/s0959-4388(97)80064-5

Source DB:  PubMed          Journal:  Curr Opin Neurobiol        ISSN: 0959-4388            Impact factor:   6.627


  95 in total

Review 1.  PDZ domains: More than just a glue.

Authors:  I Bezprozvanny; A Maximov
Journal:  Proc Natl Acad Sci U S A       Date:  2001-01-30       Impact factor: 11.205

2.  C-Terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors.

Authors:  F Steigerwald; T W Schulz; L T Schenker; M B Kennedy; P H Seeburg; G Köhr
Journal:  J Neurosci       Date:  2000-06-15       Impact factor: 6.167

3.  Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association.

Authors:  L Shen; F Liang; L D Walensky; R L Huganir
Journal:  J Neurosci       Date:  2000-11-01       Impact factor: 6.167

4.  Sticking together.

Authors:  M B Kennedy
Journal:  Proc Natl Acad Sci U S A       Date:  2000-10-10       Impact factor: 11.205

5.  cAMP-dependent protein kinase mediates activity-regulated synaptic targeting of NMDA receptors.

Authors:  F T Crump; K S Dillman; A M Craig
Journal:  J Neurosci       Date:  2001-07-15       Impact factor: 6.167

Review 6.  Molecular organization of the postsynaptic specialization.

Authors:  M Sheng
Journal:  Proc Natl Acad Sci U S A       Date:  2001-06-19       Impact factor: 11.205

7.  The novel product of a five-exon stargazin-related gene abolishes Ca(V)2.2 calcium channel expression.

Authors:  Fraser J Moss; Patricia Viard; Anthony Davies; Federica Bertaso; Karen M Page; Alex Graham; Carles Cantí; Mary Plumpton; Christopher Plumpton; Jeffrey J Clare; Annette C Dolphin
Journal:  EMBO J       Date:  2002-04-02       Impact factor: 11.598

8.  Delphilin: a novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor delta 2 subunit.

Authors:  Yohei Miyagi; Tetsuji Yamashita; Masahiro Fukaya; Tomoko Sonoda; Toshiaki Okuno; Kazuyuki Yamada; Masahiko Watanabe; Yoji Nagashima; Ichiro Aoki; Kenji Okuda; Masayoshi Mishina; Susumu Kawamoto
Journal:  J Neurosci       Date:  2002-02-01       Impact factor: 6.167

9.  Interaction with mLin-7 alters the targeting of endocytosed transmembrane proteins in mammalian epithelial cells.

Authors:  S W Straight; L Chen; D Karnak; B Margolis
Journal:  Mol Biol Cell       Date:  2001-05       Impact factor: 4.138

10.  The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the membrane-spanning proteoglycan NG2.

Authors:  D S Barritt; M T Pearn; A H Zisch; S S Lee; R T Javier; E B Pasquale; W B Stallcup
Journal:  J Cell Biochem       Date:  2000-08-02       Impact factor: 4.429

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