Glycogen Synthase Kinase 3β-mediated Phosphorylation in the Most C-terminal Region of Protein Interacting with C Kinase 1 (PICK1) Regulates the Binding of PICK1 to Glutamate Receptor Subunit GluA2

Yagishita, Sosuke; Murayama, Miyuki; Ebihara, Tomoe; Maruyama, Kei; Takashima, Akihiko

doi:10.1074/jbc.m114.619668

Cited by 32 publications

(25 citation statements)

References 29 publications

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“…Tau is localized in postsynapse, and is phosphorylated during the removal of GluA2 from synapse [75]. This removal of GluA2 requires interaction between GluA2 and PICK1 [76], which is enhanced by the presence of tau [77]. In the present study, IH28D mice exhibited a decrease in GluA2 and an increase in PICK1 to PSD-95 (Fig.…”

Section: Discussionmentioning

confidence: 61%

Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging

et al. 2017

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Sleep-disordered breathing produces cognitive impairments, and is possibly associated with Alzheimer disease (AD). Intermittent hypoxia treatment (IHT), an experimental model for sleep-disordered breathing, results in cognitive impairments in animals via unknown mechanisms. Here, we exposed mice to IHT protocols, and performed biochemical analyses and microarray analyses regarding their hippocampal samples. In particular, we performed gene ontology (GO)-based microarray analysis to elucidate effects of IHT on hippocampal functioning, which were compared with the effects of various previously-reported experimental conditions on that (ref. Gene Expression Omnibus, The National Center for Biotechnology Information). Our microarray analyses revealed that IHT and aging shared alterations in some common GO, which were also observed with kainic acid treatment, Dicer ablation, or moderate glutamate excess. Mapping the altered genes using the Kyoto Encyclopedia of Genes and Genomes PATHWAY database indicated that IHT and aging affected several pathways including “MAPK signaling pathway”, “PI3K-Akt signaling pathway”, and “glutamatergic synapse”. Consistent with the gene analyses, in vivo analyses revealed that IHT increased phosphorylated tau, reflecting an imbalance of kinases and/or phosphatases, and reduced proteins relevant to glutamatergic synapses. In addition, IHT increased phosphorylated p70 S6 kinase, indicating involvement of the mammalian target of rapamycin signaling pathway. Furthermore, IHT mice demonstrated hyperactivity in Y-maze tests, which was also observed in AD models. We obtained important data or something from the massive amount of microarray data, and confirmed the validity by in vivo analyses: the IHT-induced cognitive impairment may be partially explained by the fact that IHT increases phosphorylated tau via biological processes common to aging. Moreover, as aging is a major risk factor for AD, IHT is a novel model for investigating the pathological processes contributing to AD onset.Electronic supplementary materialThe online version of this article (doi:10.1186/s13041-016-0282-7) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 61%

Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging

et al. 2017

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“…PICK1 was originally cloned as a protein kinase Cα (PKCα) binding protein found in multiple tissues and organs, most abundantly in the brain, endocrine tissues, and skeletal muscle tissue (Human Proteome atlas). Through the PDZ domain, PICK1 interacts with a number of neurotransmitter receptors, transporters, and enzymes (Figure 7f), where in particular the interactions with the AMPAR [148][149][150][151][152][153][154][155][156][157] and the dopamine transporter (DAT) have received particular attention. Through the PDZ domain, PICK1 interacts with a number of neurotransmitter receptors, transporters, and enzymes (Figure 7f), where in particular the interactions with the AMPAR [148][149][150][151][152][153][154][155][156][157] and the dopamine transporter (DAT) have received particular attention.…”

Section: Targeting the Pdz Domain Of Protein Interacting With C Kinasementioning

confidence: 99%

PDZ Domains as Drug Targets

Christensen

Čalyševa

Fernandes

et al. 2019

Advanced Therapeutics

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Protein-protein interactions within protein networks shape the human interactome, which often is promoted by specialized protein interaction modules, such as the postsynaptic density-95 (PSD-95), discs-large, zona occludens 1 (ZO-1) (PDZ) domains. PDZ domains play a role in several cellular functions, from cell-cell communication and polarization, to regulation of protein transport and protein metabolism. PDZ domain proteins are also crucial in the formation and stability of protein complexes, establishing an important bridge between extracellular stimuli detected by transmembrane receptors and intracellular responses. PDZ domains have been suggested as promising drug targets in several diseases, ranging from neurological and oncological disorders to viral infections. In this review, the authors describe structural and genetic aspects of PDZ-containing proteins and discuss the current status of the development of small-molecule and peptide modulators of PDZ domains. An overview of potential new therapeutic interventions in PDZ-mediated protein networks is also provided.

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“…Recent studies have shown that NMDAR-induced GSK3 β phosphorylation of tau at Ser-396 is required for hippocampal LTD by enhancing the interaction between the GluA2 subunits of AMPARs with the protein interacting with C-kinase 1 (PICK1) [ 69 , 70 ], a process that is fundamental for AMPAR internalization and/or intracellular retention during LTD [ 71 – 76 ]. Furthermore, phosphorylation of PICK1 by GSK3 β at Ser-416 has also been reported to augment this interaction [ 77 ].…”

Section: Mechanisms Underlying a β -Inducedmentioning

confidence: 99%

Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking

2016

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Evidence from neuropathological, genetic, animal model, and biochemical studies has indicated that the accumulation of amyloid-beta (Aβ) is associated with, and probably induces, profound neuronal changes in brain regions critical for memory and cognition in the development of Alzheimer's disease (AD). There is considerable evidence that synapses are particularly vulnerable to AD, establishing synaptic dysfunction as one of the earliest events in pathogenesis, prior to neuronal loss. It is clear that excessive Aβ levels can disrupt excitatory synaptic transmission and plasticity, mainly due to dysregulation of the AMPA and NMDA glutamate receptors in the brain. Importantly, AMPA receptors are the principal glutamate receptors that mediate fast excitatory neurotransmission. This is essential for synaptic plasticity, a cellular correlate of learning and memory, which are the cognitive functions that are most disrupted in AD. Here we review recent advances in the field and provide insights into the molecular mechanisms that underlie Aβ-induced dysfunction of AMPA receptor trafficking. This review focuses primarily on NMDA receptor- and metabotropic glutamate receptor-mediated signaling. In particular, we highlight several mechanisms that underlie synaptic long-term depression as common signaling pathways that are hijacked by the neurotoxic effects of Aβ.

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Glycogen Synthase Kinase 3β-mediated Phosphorylation in the Most C-terminal Region of Protein Interacting with C Kinase 1 (PICK1) Regulates the Binding of PICK1 to Glutamate Receptor Subunit GluA2

Cited by 32 publications

References 29 publications

Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging

Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging

PDZ Domains as Drug Targets

Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking

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