DLG4

Last updated
DLG4
Protein DLG4 PDB 1be9.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DLG4 , PSD95, SAP-90, SAP90, Dlgh4, PSD-95, SAP90A, discs large homolog 4, discs large MAGUK scaffold protein 4, MRD62
External IDs OMIM: 602887 MGI: 1277959 HomoloGene: 1047 GeneCards: DLG4
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)

NP_001103222
NP_031890

Location (UCSC) Chr 17: 7.19 – 7.22 Mb Chr 11: 69.91 – 69.94 Mb
PubMed search [3] [4]
Wikidata
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PSD-95 (postsynaptic density protein 95) also known as SAP-90 (synapse-associated protein 90) is a protein that in humans is encoded by the DLG4 (discs large homolog 4) gene. [5] [6] [7]

Contents

PSD-95 is a member of the membrane-associated guanylate kinase (MAGUK) family. With PSD-93 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. [5] PSD-95 is the best studied member of the MAGUK-family of PDZ domain-containing proteins. Like all MAGUK-family proteins, its basic structure includes three PDZ domains, an SH3 domain, and a guanylate kinase-like domain (GK) connected by disordered linker regions. It is almost exclusively located in the post synaptic density of neurons, [8] and is involved in anchoring synaptic proteins. Its direct and indirect binding partners include neuroligin, NMDA receptors, AMPA receptors, and potassium channels. [9] It plays an important role in synaptic plasticity and the stabilization of synaptic changes during long-term potentiation. [10]

MAGUK superfamily and constituent domains

PSD-95 (encoded by DLG4) is a member of the MAGUK superfamily, and part of a subfamily which also includes PSD-93, SAP97 and SAP102. The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains. [11] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.

The PDZ domain which are contained in the MAGUKs in varying numbers, is replicated three times over in PSD-95. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. The three copies within the gene have different binding partners, due to amino acid substitutions within the PSD-95 protein and its ligands. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state. The regulatory mechanisms and function are unknown but it is hypothesized that it may involve a hook region and a calmodulin binding region located elsewhere in the gene.

Model organisms

Model organisms have been used in the study of DLG4 function. A knockout mouse line, called Dlg4tm1Grnt [19] was generated. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. [17] [20] Twenty five tests were carried out on mutant mice and seven significant abnormalities were observed. [17] Homozygous mutant animals had decreased body weight, atypical indirect calorimetry and DEXA data and a skin phenotype. Males also had abnormal plasma chemistry while females had abnormal haematology (a decreased mean corpuscular haemoglobin count). [17]

Interactions

PSD-95 has been shown to interact with:

See also

Related Research Articles

<span class="mw-page-title-main">Postsynaptic density</span>

The postsynaptic density (PSD) is a protein dense specialization attached to the postsynaptic membrane. PSDs were originally identified by electron microscopy as an electron-dense region at the membrane of a postsynaptic neuron. The PSD is in close apposition to the presynaptic active zone and ensures that receptors are in close proximity to presynaptic neurotransmitter release sites. PSDs vary in size and composition among brain regions, and have been studied in great detail at glutamatergic synapses. Hundreds of proteins have been identified in the postsynaptic density, including glutamate receptors, scaffold proteins, and many signaling molecules.

<span class="mw-page-title-main">Erbin (protein)</span> Protein found in humans

Erbb2 interacting protein (ERBB2IP), also known as erbin, is a protein which in humans is encoded by the ERBB2IP gene. Discovered in 1997, erbin is a 200kDa protein containing a PDZ domain.

<span class="mw-page-title-main">DLG1</span>

Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene.

<span class="mw-page-title-main">CASK</span> Protein-coding gene in the species Homo sapiens

Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene. This gene is also known by several other names: CMG 2, calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2. CASK gene mutations are the cause of XL-ID with our without nystagmus and MICPCH, an X-linked neurological disorder.

<span class="mw-page-title-main">PICK1</span>

Protein Interacting with C Kinase - 1 is a protein that in humans is encoded by the PICK1 gene.

<span class="mw-page-title-main">DLG3</span> Protein-coding gene in the species Homo sapiens

Disks large homolog 3 (DLG3) also known as neuroendocrine-DLG or synapse-associated protein 102 (SAP-102) is a protein that in humans is encoded by the DLG3 gene. DLG3 is a member of the membrane-associated guanylate kinase (MAGUK) superfamily of proteins.

<span class="mw-page-title-main">DLG2</span>

Disks large homolog 2 (DLG2) also known as channel-associated protein of synapse-110 (chapsyn-110) or postsynaptic density protein 93 (PSD-93) is a protein that in humans is encoded by the DLG2 gene.

<span class="mw-page-title-main">KCNA4</span>

Potassium voltage-gated channel subfamily A member 4 also known as Kv1.4 is a protein that in humans is encoded by the KCNA4 gene. It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.

<span class="mw-page-title-main">SHANK2</span>

SH3 and multiple ankyrin repeat domains protein 2 is a protein that in humans is encoded by the SHANK2 gene. Two alternative splice variants, encoding distinct isoforms, are reported. Additional splice variants exist but their full-length nature has not been determined.

<span class="mw-page-title-main">DLGAP1</span>

Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP), is a protein that in humans is encoded by the DLGAP1 gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the post-synaptic density.

<span class="mw-page-title-main">SHANK1</span> Protein-coding gene in the species Homo sapiens

SH3 and multiple ankyrin repeat domains protein 1 is a protein that in humans is encoded by the SHANK1 gene.

<span class="mw-page-title-main">LIN7A</span>

Lin-7 homolog A is a protein that in humans is encoded by the LIN7A gene.

<span class="mw-page-title-main">MAGI2</span>

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 also known as membrane-associated guanylate kinase inverted 2 (MAGI-2) and atrophin-1-interacting protein 1 (AIP-1) is an enzyme that in humans is encoded by the MAGI2 gene.

<span class="mw-page-title-main">DLGAP4</span> Protein-coding gene in the species Homo sapiens

Disks large-associated protein 4 (DAP-4) also known as SAP90/PSD-95-associated protein 4 (SAPAP-4) is a protein that in humans is encoded by the DLGAP4 gene.

<span class="mw-page-title-main">LIN7B</span> Protein-coding gene in humans

Lin-7 homolog B is a protein that in humans is encoded by the LIN7B gene.

<span class="mw-page-title-main">DLGAP2</span> Protein-coding gene in the species Homo sapiens

Disks large-associated protein 2 is a protein that in humans is encoded by the DLGAP2 gene.

<span class="mw-page-title-main">CRIPT</span>

Cysteine-rich PDZ-binding protein is a protein that in humans is encoded by the CRIPT gene.

<span class="mw-page-title-main">CNKSR2</span> Protein-coding gene in the species Homo sapiens

Connector enhancer of kinase suppressor of ras 2, also known as CNK homolog protein 2 (CNK2) or maguin, is an enzyme that in humans is encoded by the CNKSR2 gene.

The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins. The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains. The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein–protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.

<span class="mw-page-title-main">Mary B. Kennedy</span> American biochemist and neuroscientist

Mary Bernadette Kennedy is an American biochemist and neuroscientist. She is a member of the American Academy of Arts and Sciences, and is the Allen and Lenabelle Davis Professor of Biology at the California Institute of Technology, where she has been a member of the faculty since 1981. Her research focuses on the molecular mechanisms of synaptic plasticity, the process underlying formation of memory in the central nervous system. Her lab uses biochemical and molecular biological methods to study the protein machinery within a structure called the postsynaptic density. Kennedy has published over 100 papers with over 20,000 total citations.

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