δ-Catenin Regulates Spine Architecture via Cadherin and PDZ-dependent Interactions

Li, Yuan; Seong, Eunju; Beuscher, James L.; Arikkath, Jyothi

doi:10.1074/jbc.m114.632679

Cited by 30 publications

(48 citation statements)

References 56 publications

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“…In neurons, δ-catenin interacts with N-cadherin, glutamate receptors at PSD, and PSD95, as well as a whole array of other synaptic junction associated proteins (Lu et al 1999; Ide et al 1999; Jones et al 2002; Silverman et al 2007; Brigidi et al 2014; Yuan et al 2015). Based on all the known protein binding partners for δ-catenin, it strongly suggests that δ-catenin plays important roles in brain functions that involve synaptic regulation, especially learning and emotions according to a gene deletion study (Israely et al 2004).…”

Section: Discovery Of δ-Cateninmentioning

confidence: 99%

“…Based on all the known protein binding partners for δ-catenin, it strongly suggests that δ-catenin plays important roles in brain functions that involve synaptic regulation, especially learning and emotions according to a gene deletion study (Israely et al 2004). Indeed, δ-catenin knockdown regulates spine architecture related to cadherin and PDZ-dependent interactions (Yuan et al 2015). A gene knockout (KO) study revealed that δ-catenin is required for the maintenance of neural structure and function in mature cortex in vivo (Matter et al 2009).…”

Section: Discovery Of δ-Cateninmentioning

confidence: 99%

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Genetic alterations of δ-catenin/NPRAP/Neurojungin (CTNND2): functional implications in complex human diseases

Lü

Aguilar

et al. 2016

Hum Genet

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Some genes involved in complex human diseases are particularly vulnerable to genetic variations such as single nucleotide polymorphism, copy number variations, and mutations. For example, Ras mutations account for over 30% of all human cancers. Additionally, there are some genes that can display different variations with functional impact in different diseases that are unrelated. One such gene stands out: δ-catenin/NPRAP/Neurojungin with gene designation as CTNND2 on chromosome 5p15.2. Recent advances in genome wide association as well as molecular biology approaches have uncovered striking involvement of δ-catenin gene variations linked to complex human disorders. These disorders include cancer, bipolar disorder, schizophrenia, autism, Cri-du-chat syndrome, myopia, cortical cataract-linked Alzheimer’s disease, and infectious diseases. This list has rapidly grown longer in recent years, underscoring the pivotal roles of δ-catenin in critical human diseases. δ-Catenin is an adhesive junction-associated protein in the delta subfamily of the β-catenin superfamily. δ-Catenin functions in Wnt signaling to regulate gene expression and modulate Rho GTPases of the Ras superfamily in cytoskeletal reorganization. δ-Catenin likely lies where Wnt signaling meets Rho GTPases and is a unique and vulnerable common target for mutagenesis in different human diseases.

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Section: Discovery Of δ-Cateninmentioning

confidence: 99%

Section: Discovery Of δ-Cateninmentioning

confidence: 99%

Genetic alterations of δ-catenin/NPRAP/Neurojungin (CTNND2): functional implications in complex human diseases

Lü

Aguilar

et al. 2016

Hum Genet

View full text Add to dashboard Cite

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“…δ-catenin (also called neural plakophilin-related armadillo protein, NPRAP) is a neuron-specific catenin that also binds the cadherin intracellular domain, proximal to the plasma membrane (Kosik et al , 2005; Paffenholz and Franke, 1997). The ARM domains of δ-catenin mediate interaction with N-cadherin (Silverman et al , 2007) and the carboxyl terminus of δ-catenin binds to PDZ domains of two related scaffolds, AMPAR-binding protein (ABP) and glutamate receptor-interaction protein (GRIP) (Kosik et al , 2005; Silverman et al , 2007; Yuan et al , 2015) (Fig. 1a).…”

Section: Introductionmentioning

confidence: 99%

“…1a). Thus, δ-catenin forms a bridge at synapses between cadherins and the ABP and GRIP scaffolds and associated GluA2/3-containing AMPARs (Silverman et al , 2007; Yuan et al , 2015) (Fig. 1a).…”

Section: Introductionmentioning

confidence: 99%

“…δ-catenin knockout (KO) mice show impairments in hippocampal synaptic plasticity, including short-term and long-term plasticity, which is strongly associated with severe defects in cognitive function (Israely et al , 2004). Furthermore, N-cadherin, PSD-95 (post synaptic density-95), and GluA2 are significantly reduced, contributing to spine loss in the hippocampal synapse of the mutant animal (Israely et al , 2004; Restituito et al , 2011; Yuan et al , 2015). A recent study shows that loss of δ-catenin function by missense mutations causes severe autism (Turner et al , 2015).…”

Section: Introductionmentioning

confidence: 99%

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Lithium increases synaptic GluA2 in hippocampal neurons by elevating the δ-catenin protein

et al. 2017

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Lithium (Li+) is a drug widely employed for treating bipolar disorder, however the mechanism of action is not known. Here we study the effects of Li+ in cultured hippocampal neurons on a synaptic complex consisting of δ-catenin, a protein associated with cadherins whose mutation is linked to autism, and GRIP, an AMPA receptor (AMPAR) scaffolding protein, and the AMPAR subunit, GluA2. We show that Li+ elevates the level of δ-catenin in cultured neurons. δ-catenin binds to the ABP and GRIP proteins, which are synaptic scaffolds for GluA2. We show that Li+ increases the levels of GRIP and GluA2, consistent with Li+-induced elevation of δ-catenin. Using GluA2 mutants, we show that the increase in surface level of GluA2 requires GluA2 interaction with GRIP. The amplitude but not the frequency of mEPSCs was also increased by Li+ in cultured hippocampal neurons, confirming a functional effect and consistent with AMPAR stabilization at synapses. Furthermore, animals fed with Li+ show elevated synaptic levels of δ-catenin, GRIP, and GluA2 in the hippocampus, also consistent with the findings in cultured neurons. This work supports a model in which Li+ stabilizes δ-catenin, thus elevating a complex consisting of δ-catenin, GRIP and AMPARs in synapses of hippocampal neurons. Thus, the work suggests a mechanism by which Li+ can alter brain synaptic function that may be relevant to its pharmacologic action in treatment of neurological disease.

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5p deletions: Current knowledge and future directions

Nguyen¹,

Qualmann²,

Okashah³

et al. 2015

American J of Med Genetics Pt C

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Disorders resulting from 5p deletions (5p–) were first recognized by Lejeune et al. in 1963 [Lejeune et al. (1963); C R Hebd Seances Acad Sci 257:3098-3102]. 5p– is caused by partial or total deletion of the short arm of chromosome 5. The most recognizable phenotype is characterized by a high-pitched cry, dysmorphic features, poor growth, and developmental delay. This report reviews 5p– disorders and their molecular basis. Hemizygosity for genes located within this region have been implicated in contributing to the phenotype. A review of the genes on 5p which may be dosage sensitive is summarized. Because of the growing knowledge of these specific genes, future directions to explore potential targeted therapies for individuals with 5p– are discussed.

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δ-Catenin Regulates Spine Architecture via Cadherin and PDZ-dependent Interactions

Cited by 30 publications

References 56 publications

Genetic alterations of δ-catenin/NPRAP/Neurojungin (CTNND2): functional implications in complex human diseases

Genetic alterations of δ-catenin/NPRAP/Neurojungin (CTNND2): functional implications in complex human diseases

Lithium increases synaptic GluA2 in hippocampal neurons by elevating the δ-catenin protein

5p deletions: Current knowledge and future directions

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