Glutamate-induced δ-catenin redistribution and dissociation from postsynaptic receptor complexes

Jones, Shiloh B.; Lanford, George W.; Chen, Y.-H; Moribito, M; Kim, K; Lü, Qun

doi:10.1016/s0306-4522(02)00532-8

Cited by 49 publications

(37 citation statements)

References 29 publications

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“…Competition among Shank, D-catenin, and Densin-180 is likely to occur in vivo at synapses, because all three proteins are enriched in the PSD fraction (Apperson et al, 1996;Naisbitt et al, 1999;Jones et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Postsynaptic Shank Antagonizes Dendrite Branching Induced by the Leucine-Rich Repeat Protein Densin-180

et al. 2005

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Section: Discussionmentioning

confidence: 99%

Postsynaptic Shank Antagonizes Dendrite Branching Induced by the Leucine-Rich Repeat Protein Densin-180

et al. 2005

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“…Embryonic hippocampal cultures were prepared as described by Goslin and colleagues with minor modifications (Goslin et al, 1998;Jones et al, 2002;Lu et al, 2002). Briefly, 18 d timed pregnant rats were killed, and the embryos were removed in accordance with the National Institutes of Health Guide for the Care and Use of Laboratory Animals.…”

Section: Methodsmentioning

confidence: 99%

Abl Tyrosine Kinase Promotes Dendrogenesis by Inducing Actin Cytoskeletal Rearrangements in Cooperation with Rho Family Small GTPases in Hippocampal Neurons

Jones¹,

Lu²,

Lü³

2004

J. Neurosci.

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Nonreceptor tyrosine kinase Abl is an actin-binding protein and a key regulator of neuronal axonal development. Although Abl family kinases also are localized in dendrites and are implicated in postsynaptic functions, it is not clear how Abl kinases regulate dendritic morphogenesis. Using a developing hippocampal culture as a model, we found that the inhibition of Abl kinases by STI571 leads to a remarkable simplification of dendritic branching similar to the phenotype caused by an increased activity of small GTPase RhoA. Time-lapse microscopic imaging reveals a prominent reduction of dendritic branching. In contrast, neurons expressing a constitutively active v-abl construct (CA-Abl) show an exuberant microtubule-associated protein 2-positive (MAP2-positive) dendrite outgrowth, suggesting that Abl modulates dendritic growth. Biochemical assays using a glutathione S-transferase pull-down method to determine GTP-bound active Rho GTPases demonstrate that Abl inhibition increases RhoA activity but has no effect on the activity of Rac1 or Cdc42. At the cellular level the alteration of Abl also changes actin organization consistent with RhoA inhibition. Suppression of the RhoA downstream effector Rho kinase reverses STI571-induced dendritic simplification, demonstrating that activity of the Rho pathway is responsible for the Abl-induced changes in dendrogenesis. Furthermore, CA-Abl-induced neurite outgrowth is blocked by the expression of a constitutively active RhoA construct. The CA-Abl phenotype is not affected by destabilization of microtubules but is reversed partially when actin filaments are stabilized with jasplakinolide. Together, these studies support a critical role for Abl kinases in regulating dendrogenesis by inducing actin cytoskeletal rearrangements in cooperation with Rho GTPases.

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“…δ-Catenin is highly expressed in the dendrites of the mature brain [10]. The induction of branching of dendrite-like processes by overexpressed δ-catenin suggests its role in dendrogenesis and brain functions [11].It is worth noting that PS-1 is detected in neuronal processes and filopodia-like structures of growth cones in a primary culture of rat hippocampal neurons where δ-catenin is also localized [2].…”

Section: Discussionmentioning

confidence: 98%

“…In this scenario, δ-catenin has to be in the vicinity of the PS-1/γ-secretase complex physically. Indeed, δ-catenin is enriched in the postsynaptic junction where PS-1 is also localized and δ-catenin interacts with glutamate receptors (NR2A and mGluR1α) and postsynaptic protein-95 (PSD-95) [10].On the other hand, δ-catenin may be processed by an as yet unidentified protease that is activated by PS-1/γ-secretase activity. In this case, no direct γ-secretase-like activity exists for δ-catenin.…”

Section: Discussionmentioning

confidence: 99%

Presenilin-1 inhibits δ-catenin-induced cellular branching and promotes δ-catenin processing and turnover

Kim

Bareiss

Kim

et al. 2006

Biochemical and Biophysical Research Communications

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Although δ-catenin/neural plakophilin-related armadillo protein (NPRAP) was reported to interact with presenilin-1 (PS-1), the effects of PS-1 on δ-catenin have not been established. In this study, we report that overexpression of PS-1 inhibits the δ-catenin-induced dendrite-like morphological changes in NIH 3T3 cells and promotes δ-catenin processing and turnover. The effects of PS-1 on endogenous δ-catenin processing were confirmed in hippocampal neurons overexpressing PS-1, as well as in the transgenic mice expressing the disease-causing mutant PS-1 (M146V). In addition, disease-causing mutant PS-1 (M146V and L286V) enhanced δ-catenin processing, whereas PS-1/γ-secretase inhibitors could block the formation of processed forms of δ-catenin. Together, our findings suggest that PS-1 can affect δ-catenin-induced morphogenesis possibly through the regulation of its processing and stability. KeywordsAlzheimer's disease; δ-Catenin/NPRAP; Presenilin/γ-secretase Alzheimer's disease (AD) is the most common type of senile dementia and is characterized by progressive loss of memory and cognitive dysfunction [16]. In familial Alzheimer's disease (FAD), over 70 mutations have been significantly associated with presenilin-1 (PS-1) and presenilin-2 (PS-2) [7]. Multiple lines of evidence indicate that PS contributes directly to the intramembranous "γ-secretase" processing of many proteins of diverse functions, including APP [3], the developmental signaling receptor Notch1 [4], and cell adhesion molecules N-and E-cadherin [15]. Interestingly, it is reported that PS-1 interacts with a member of the armadillo/ β-catenin family termed δ-catenin, a protein expressed mostly in the brain and encoded on chromosome 5 [21]. δ-Catenin, or neural plakophilin-related armadillo protein (NPRAP), is a member of the p120 ctn subfamily of armadillo/β-catenin proteins, which are defined as proteins with 10 armadillo (ARM) repeats in characteristic spacing and with diverse NH 2 -and COOH-terminal sequences that flank the ARM repeats [18]. δ-Catenin is a nervous system-specific adherens junction protein involved in cell motility and expressed early in neuronal development [14]. The overexpression of δ-catenin can induce the branching of cellular processes in 3T3 cells In this report, we investigated the effects of PS-1 on δ-catenin. The co-overexpressed PS-1 significantly impaired δ-catenin-induced cellular branching in NIH 3T3 fibroblasts. We also found that PS-1 expression promoted δ-catenin processing when they were co-transfected in 3T3 cells and when PS-1 was overexpressed in hippocampal neurons, which was sensitive to PS-1/γ-secretase inhibition and was facilitated by the Alzheimer's disease-causing PS-1 mutation. Our findings suggest that one function of PS-1 expression is to promote δ-catenin processing and, thereby, affect the function of δ-catenin in cells. Experimental procedures Plasmid constructionConstruction of full-length-δ-catenin constructs in pEGFP-C1 or pRFP-C1 has been described previously [11]. The wild-type PS-1 and...

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Glutamate-induced δ-catenin redistribution and dissociation from postsynaptic receptor complexes

Cited by 49 publications

References 29 publications

Postsynaptic Shank Antagonizes Dendrite Branching Induced by the Leucine-Rich Repeat Protein Densin-180

Postsynaptic Shank Antagonizes Dendrite Branching Induced by the Leucine-Rich Repeat Protein Densin-180

Abl Tyrosine Kinase Promotes Dendrogenesis by Inducing Actin Cytoskeletal Rearrangements in Cooperation with Rho Family Small GTPases in Hippocampal Neurons

Presenilin-1 inhibits δ-catenin-induced cellular branching and promotes δ-catenin processing and turnover

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