Research article summary (published 29 Apr 1997):

Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95.

Full Abstract

The PSD-95/SAP90 family of PDZ-containing proteins is directly involved in the clustering of specific ion channels at synapses. We report that channel clustering depends on a conserved N-terminal domain of PSD-95 that mediates multimerization and disulfide linkage of PSD-95 protomers. This N-terminal multimerization domain confers channel clustering activity on a single PDZ domain. Thus, channel clustering depends on aggregation of PDZ domains achieved by head-to-head multimerization of PSD-95, rather than by concatenation of PDZ domains in PSD-95 monomers. This mechanism predicts that PSD-95 can organize heterogeneous membrane protein clusters via differential binding specificities of its three PDZ domains. PSD-95 and its relative chapsyn-110 exist as disulfide-linked complexes in rat brain, consistent with head-to-head multimerization of these proteins in vivo.

Author information

Author/s: Hsueh, Y P (YP); Kim, E (E); Sheng, M (M);

Affiliation: Howard Hughes Medical Institute and Department of Neurobiology, Massachusetts General Hospital and Harvard Medical School, Boston 02214, USA.

Journal and publication information

Publication Type: Journal Article

Journal: Neuron (Neuron), published in UNITED STATES. (Language: eng)

Reference: 1997-May; vol 18 (issue 5) : pp 803-14

Dates: Created 1997/06/30; Completed 1997/06/30; Revised 2005/11/17;

PMID: 9182804, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals COS Cells - chemistry; physiology Cross-Linking Reagents - chemistry; metabolism Disulfides - chemistry; metabolism Gene Deletion Guanylate Kinase Intracellular Signaling Peptides and Proteins Ligands Membrane Proteins Molecular Sequence Data Mutagenesis - physiology

Nerve Tissue Proteins - chemistry; genetics; physiology Nucleoside-Phosphate Kinase - genetics; metabolism Potassium Channels - chemistry; metabolism Precipitin Tests Protein Binding - physiology Protein Structure, Tertiary Rats Sequence Homology, Amino Acid Shaker Superfamily of Potassium Channels Transfection Tumor Suppressor Proteins

Associated Chemicals: Cross-Linking Reagents (0) ; Disulfides (0) ; Dlgh4 protein, rat (0) ; Intracellular Signaling Peptides and Proteins (0) ; Ligands (0) ; Membrane Proteins (0) ; Mpp2 protein, rat (0) ; Nerve Tissue Proteins (0) ; Potassium Channels (0) ; Shaker Superfamily of Potassium Channels (0) ; Tumor Suppressor Proteins (0) ; postsynaptic density proteins (0) ; Nucleoside-Phosphate Kinase (EC 2.7.4.4) ; DLG2 protein, human (EC 2.7.4.8) ; Guanylate Kinase (EC 2.7.4.8)

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