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Article: Phosphorylation of the AMPAR-TARP Complex in Synaptic Plasticity.

Park, Joongkyu

2018 Volume 6, Issue 4

Abstract: Synaptic plasticity has been considered a key mechanism underlying many brain functions including learning, memory, and drug addiction. An increase or decrease in synaptic activity of the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor ( ... ...

Abstract	Synaptic plasticity has been considered a key mechanism underlying many brain functions including learning, memory, and drug addiction. An increase or decrease in synaptic activity of the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) complex mediates the phenomena as shown in the cellular models of synaptic plasticity, long-term potentiation (LTP), and depression (LTD). In particular, protein phosphorylation shares the spotlight in expressing the synaptic plasticity. This review summarizes the studies on phosphorylation of the AMPAR pore-forming subunits and auxiliary proteins including transmembrane AMPA receptor regulatory proteins (TARPs) and discusses its role in synaptic plasticity.
Language	English
Publishing date	2018-10-08
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2720995-7
ISSN	2227-7382
ISSN	2227-7382
DOI	10.3390/proteomes6040040
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: NMDA receptor-targeted enrichment of CaMKIIα improves fear memory.

Chifor, Anthony / Choi, Jeongyoon / Park, Joongkyu

iScience

2022 Volume 25, Issue 8, Page(s) 104864

Abstract: The establishment of effective molecular interventions to improve memory and alleviate memory deficits in disease remains a long-standing challenge despite growing molecular understanding of synaptic plasticity and memory formation. Capitalizing on the ... ...

Abstract	The establishment of effective molecular interventions to improve memory and alleviate memory deficits in disease remains a long-standing challenge despite growing molecular understanding of synaptic plasticity and memory formation. Capitalizing on the fact that long-term potentiation (LTP) requires N-methyl-D-aspartate receptors (NMDARs) and Ca
Language	English
Publishing date	2022-08-02
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2022.104864
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Article ; Online: Chemogenetic regulation of the TARP-lipid interaction mimics LTP and reversibly modifies behavior.

Park, Joongkyu / Berthoux, Coralie / Hoyos-Ramirez, Erika / Shan, Lili / Morimoto-Tomita, Megumi / Wang, Yixiang / Castillo, Pablo E / Tomita, Susumu

Cell reports

2023 Volume 42, Issue 8, Page(s) 112826

Abstract: Long-term potentiation (LTP), a well-characterized form of synaptic plasticity, is believed to underlie memory formation. Hebbian, postsynaptically expressed LTP requires TARPγ-8 phosphorylation for synaptic insertion of AMPA receptors (AMPARs). However, ...

Abstract	Long-term potentiation (LTP), a well-characterized form of synaptic plasticity, is believed to underlie memory formation. Hebbian, postsynaptically expressed LTP requires TARPγ-8 phosphorylation for synaptic insertion of AMPA receptors (AMPARs). However, it is unknown whether TARP-mediated AMPAR insertion alone is sufficient to modify behavior. Here, we report the development of a chemogenetic tool, ExSYTE (Excitatory SYnaptic Transmission modulator by Engineered TARPγ-8), to mimic the cytoplasmic interaction of TARP with the plasma membrane in a doxycycline-dependent manner. We use this tool to examine the specific role of synaptic AMPAR potentiation in amygdala neurons that are activated by fear conditioning. Selective expression of active ExSYTE in these neurons potentiates AMPAR-mediated synaptic transmission in a doxycycline-dependent manner, occludes synaptically induced LTP, and mimics freezing triggered by cued fear conditioning. Thus, chemogenetic controlling of the TARP-membrane interaction is sufficient for LTP-like synaptic AMPAR insertion, which mimics fear conditioning.
MeSH term(s)	Long-Term Potentiation/physiology ; Doxycycline/pharmacology ; Synapses/metabolism ; Synaptic Transmission ; Lipids
Chemical Substances	TARP ; Doxycycline (N12000U13O) ; Lipids
Language	English
Publishing date	2023-07-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112826
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Article ; Online: The Troyer syndrome protein spartin mediates selective autophagy of lipid droplets.

Chung, Jeeyun / Park, Joongkyu / Lai, Zon Weng / Lambert, Talley J / Richards, Ruth C / Zhang, Jiuchun / Walther, Tobias C / Farese, Robert V

Nature cell biology

2023 Volume 25, Issue 8, Page(s) 1101–1110

Abstract: Lipid droplets (LDs) are crucial organelles for energy storage and lipid homeostasis. Autophagy of LDs is an important pathway for their catabolism, but the molecular mechanisms mediating LD degradation by selective autophagy (lipophagy) are unknown. ... ...

Abstract	Lipid droplets (LDs) are crucial organelles for energy storage and lipid homeostasis. Autophagy of LDs is an important pathway for their catabolism, but the molecular mechanisms mediating LD degradation by selective autophagy (lipophagy) are unknown. Here we identify spartin as a receptor localizing to LDs and interacting with core autophagy machinery, and we show that spartin is required to deliver LDs to lysosomes for triglyceride mobilization. Mutations in SPART (encoding spartin) lead to Troyer syndrome, a form of complex hereditary spastic paraplegia
MeSH term(s)	Mice ; Humans ; Animals ; Spastic Paraplegia, Hereditary/genetics ; Spastic Paraplegia, Hereditary/metabolism ; Lipid Droplets/metabolism ; Cell Cycle Proteins/metabolism ; Carrier Proteins/metabolism ; Autophagy ; Triglycerides/metabolism ; Lipid Metabolism/physiology
Chemical Substances	Cell Cycle Proteins ; Carrier Proteins ; Triglycerides
Language	English
Publishing date	2023-07-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-023-01178-w
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Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Chemogenetic regulation of the TARP-lipid interaction mimics LTP and reversibly modifies behavior

Joongkyu Park / Coralie Berthoux / Erika Hoyos-Ramirez / Lili Shan / Megumi Morimoto-Tomita / Yixiang Wang / Pablo E. Castillo / Susumu Tomita

Cell Reports, Vol 42, Iss 8, Pp 112826- (2023)

2023

Abstract: Summary: Long-term potentiation (LTP), a well-characterized form of synaptic plasticity, is believed to underlie memory formation. Hebbian, postsynaptically expressed LTP requires TARPγ-8 phosphorylation for synaptic insertion of AMPA receptors (AMPARs). ...

Abstract	Summary: Long-term potentiation (LTP), a well-characterized form of synaptic plasticity, is believed to underlie memory formation. Hebbian, postsynaptically expressed LTP requires TARPγ-8 phosphorylation for synaptic insertion of AMPA receptors (AMPARs). However, it is unknown whether TARP-mediated AMPAR insertion alone is sufficient to modify behavior. Here, we report the development of a chemogenetic tool, ExSYTE (Excitatory SYnaptic Transmission modulator by Engineered TARPγ-8), to mimic the cytoplasmic interaction of TARP with the plasma membrane in a doxycycline-dependent manner. We use this tool to examine the specific role of synaptic AMPAR potentiation in amygdala neurons that are activated by fear conditioning. Selective expression of active ExSYTE in these neurons potentiates AMPAR-mediated synaptic transmission in a doxycycline-dependent manner, occludes synaptically induced LTP, and mimics freezing triggered by cued fear conditioning. Thus, chemogenetic controlling of the TARP-membrane interaction is sufficient for LTP-like synaptic AMPAR insertion, which mimics fear conditioning.
Keywords	CP: Neuroscience ; CP: Cell biology ; Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2023-08-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Protein phosphatase PPM1B inhibits DYRK1A kinase through dephosphorylation of pS258 and reduces toxic tau aggregation.

Lee, Ye Hyung / Im, Eunju / Hyun, Minju / Park, Joongkyu / Chung, Kwang Chul

The Journal of biological chemistry

2021 Volume 296, Page(s) 100245

Abstract: Down syndrome (DS) is mainly caused by an extra copy of chromosome 21 (trisomy 21), and patients display a variety of developmental symptoms, including characteristic facial features, physical growth delay, intellectual disability, and neurodegeneration ( ...

Abstract	Down syndrome (DS) is mainly caused by an extra copy of chromosome 21 (trisomy 21), and patients display a variety of developmental symptoms, including characteristic facial features, physical growth delay, intellectual disability, and neurodegeneration (i.e., Alzheimer's disease; AD). One of the pathological hallmarks of AD is insoluble deposits of neurofibrillary tangles (NFTs) that consist of hyperphosphorylated tau. The human DYRK1A gene is mapped to chromosome 21, and the protein is associated with the formation of inclusion bodies in AD. For example, DYRK1A directly phosphorylates multiple serine and threonine residues of tau, including Thr212. However, the mechanism underpinning DYRK1A involvement in Trisomy 21-related pathological tau aggregation remains unknown. Here, we explored a novel regulatory mechanism of DYRK1A and subsequent tau pathology through a phosphatase. Using LC-MS/MS technology, we analyzed multiple DYRK1A-binding proteins, including PPM1B, a member of the PP2C family of Ser/Thr protein phosphatases, in HEK293 cells. We found that PPM1B dephosphorylates DYRK1A at Ser258, contributing to the inhibition of DYRK1A activity. Moreover, PPM1B-mediated dephosphorylation of DYRK1A reduced tau phosphorylation at Thr212, leading to inhibition of toxic tau oligomerization and aggregation. In conclusion, our study demonstrates that DYRK1A autophosphorylates Ser258, the dephosphorylation target of PPM1B, and PPM1B negatively regulates DYRK1A activity. This finding also suggests that PPM1B reduces the toxic formation of phospho-tau protein via DYRK1A modulation, possibly providing a novel cellular protective mechanism to regulate toxic tau-mediated neuropathology in AD of DS.
MeSH term(s)	Alzheimer Disease/complications ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Carrier Proteins/genetics ; Chromatography, Liquid ; Down Syndrome/complications ; Down Syndrome/genetics ; Down Syndrome/pathology ; HEK293 Cells ; Humans ; Nerve Degeneration ; Neurofibrillary Tangles/genetics ; Neurofibrillary Tangles/pathology ; Phosphoprotein Phosphatases/genetics ; Phosphorylation/genetics ; Protein Aggregation, Pathological/genetics ; Protein Phosphatase 2C/genetics ; Protein Serine-Threonine Kinases/genetics ; Protein-Tyrosine Kinases/genetics ; Tandem Mass Spectrometry ; tau Proteins/genetics ; Dyrk Kinases
Chemical Substances	Carrier Proteins ; tau Proteins ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; PPM1B protein, human (EC 3.1.3.16) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 2C (EC 3.1.3.16)
Language	English
Publishing date	2021-01-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.015574
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Article: New Perspectives of Dyrk1A Role in Neurogenesis and Neuropathologic Features of Down Syndrome.

Park, Joongkyu / Chung, Kwang Chul

Experimental neurobiology

2013 Volume 22, Issue 4, Page(s) 244–248

Abstract: Down syndrome (DS) is one of the most common genetic disorders accompanying with mental retardation, cognitive impairment, and deficits in learning and memory. The brains with DS also display many neuropathological features including alteration in ... ...

Abstract	Down syndrome (DS) is one of the most common genetic disorders accompanying with mental retardation, cognitive impairment, and deficits in learning and memory. The brains with DS also display many neuropathological features including alteration in neurogenesis and synaptogenesis and early onset of Alzheimer's disease (AD)-like symptoms. Triplication of all or a part of human chromosome 21, especially the 21q22.1~21q22.3 region called 'Down syndrome critical region (DSCR)', has been considered as the main cause of DS. One gene product of DSCR, dual-specificity tyrosine-phosphorylation-regulated kinase 1A (Dyrk1A), has been highlighted as a key contributor to the neural consequences of DS. This minireview summarizes accumulating recent reports about Dyrk1A involvement in the neuritogenesis, synaptogenesis, and AD-like neurofibrillary tangle formation, which is mainly focusing on Dyrk1A-mediated regulation of cytoskeletal proteins, such as tubulin, actin, and microtubule-associated protein tau. Understanding the molecular mechanisms of these phenomena may provide us a rational for new preventive and therapeutic treatment of DS.
Language	English
Publishing date	2013-12-31
Publishing country	Korea (South)
Document type	Journal Article ; Review
ZDB-ID	2639017-6
ISSN	2093-8144 ; 1226-2560
ISSN (online)	2093-8144
ISSN	1226-2560
DOI	10.5607/en.2013.22.4.244
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Article ; Online: TMEM163 Regulates ATP-Gated P2X Receptor and Behavior.

Salm, Elizabeth J / Dunn, Patrick J / Shan, Lili / Yamasaki, Miwako / Malewicz, Nathalie M / Miyazaki, Taisuke / Park, Joongkyu / Sumioka, Akio / Hamer, R Richard L / He, Wei-Wu / Morimoto-Tomita, Megumi / LaMotte, Robert H / Tomita, Susumu

Cell reports

2020 Volume 31, Issue 9, Page(s) 107704

Abstract: Fast purinergic signaling is mediated by ATP and ATP-gated ionotropic P2X receptors (P2XRs), and it is implicated in pain-related behaviors. The properties exhibited by P2XRs vary between those expressed in heterologous cells and in vivo. Several ... ...

Abstract	Fast purinergic signaling is mediated by ATP and ATP-gated ionotropic P2X receptors (P2XRs), and it is implicated in pain-related behaviors. The properties exhibited by P2XRs vary between those expressed in heterologous cells and in vivo. Several modulators of ligand-gated ion channels have recently been identified, suggesting that there are P2XR functional modulators in vivo. Here, we establish a genome-wide open reading frame (ORF) collection and perform functional screening to identify modulators of P2XR activity. We identify TMEM163, which specifically modulates the channel properties and pharmacology of P2XRs. We also find that TMEM163 is required for full function of the neuronal P2XR and a pain-related ATP-evoked behavior. These results establish TMEM163 as a critical modulator of P2XRs in vivo and a potential target for the discovery of drugs for treating pain.
MeSH term(s)	Adenosine Triphosphate/pharmacology ; Animals ; Behavior, Animal/drug effects ; Calcium/metabolism ; Evoked Potentials/drug effects ; Female ; Genome ; HEK293 Cells ; Humans ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurons/metabolism ; Open Reading Frames/genetics ; Pain/pathology ; RNA Interference ; RNA, Small Interfering/metabolism ; Receptors, Purinergic P2X/genetics ; Receptors, Purinergic P2X/metabolism ; Receptors, Purinergic P2X3/deficiency ; Receptors, Purinergic P2X3/genetics ; Receptors, Purinergic P2X3/metabolism
Chemical Substances	Membrane Proteins ; RNA, Small Interfering ; Receptors, Purinergic P2X ; Receptors, Purinergic P2X3 ; Tmem163 protein, mouse ; Adenosine Triphosphate (8L70Q75FXE) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2020-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.107704
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Article ; Online: TMEM163 Regulates ATP-Gated P2X Receptor and Behavior

Elizabeth J. Salm / Patrick J. Dunn / Lili Shan / Miwako Yamasaki / Nathalie M. Malewicz / Taisuke Miyazaki / Joongkyu Park / Akio Sumioka / R. Richard L. Hamer / Wei-Wu He / Megumi Morimoto-Tomita / Robert H. LaMotte / Susumu Tomita

Cell Reports, Vol 31, Iss 9, Pp - (2020)

2020

Abstract: Summary: Fast purinergic signaling is mediated by ATP and ATP-gated ionotropic P2X receptors (P2XRs), and it is implicated in pain-related behaviors. The properties exhibited by P2XRs vary between those expressed in heterologous cells and in vivo. ... ...

Abstract	Summary: Fast purinergic signaling is mediated by ATP and ATP-gated ionotropic P2X receptors (P2XRs), and it is implicated in pain-related behaviors. The properties exhibited by P2XRs vary between those expressed in heterologous cells and in vivo. Several modulators of ligand-gated ion channels have recently been identified, suggesting that there are P2XR functional modulators in vivo. Here, we establish a genome-wide open reading frame (ORF) collection and perform functional screening to identify modulators of P2XR activity. We identify TMEM163, which specifically modulates the channel properties and pharmacology of P2XRs. We also find that TMEM163 is required for full function of the neuronal P2XR and a pain-related ATP-evoked behavior. These results establish TMEM163 as a critical modulator of P2XRs in vivo and a potential target for the discovery of drugs for treating pain.
Keywords	ion channel ; P2X receptor ; ATP ; modulator ; channel ; pharmacology ; Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2020-06-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Function and regulation of Dyrk1A: towards understanding Down syndrome.

Park, Joongkyu / Song, Woo-Joo / Chung, Kwang Chul

Cellular and molecular life sciences : CMLS

2009 Volume 66, Issue 20, Page(s) 3235–3240

Abstract: Down syndrome (DS) is associated with a variety of symptoms, such as incapacitating mental retardation and neurodegeneration (i.e., Alzheimer's disease), that prevent patients from leading fully independent lives. These phenotypes are a direct ... ...

Abstract	Down syndrome (DS) is associated with a variety of symptoms, such as incapacitating mental retardation and neurodegeneration (i.e., Alzheimer's disease), that prevent patients from leading fully independent lives. These phenotypes are a direct consequence of the overexpression of chromosome 21 genes, which are present in duplicate due to non-disjunction of chromosome 21. Accumulating data suggest that the chromosome 21 gene product, dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1A (Dyrk1A), participates in the pathogenic mechanisms underlying the mental and other physical symptoms of DS. In this review, we summarize the evidence supporting a role for Dyrk1A in DS, especially DS pathogenesis. Recently, several natural and synthetic compounds have been identified as Dyrk1A inhibitors. Understanding the function and regulation of Dyrk1A may lead to the development of novel therapeutic agents aimed at treating DS.
MeSH term(s)	Animals ; Chromosomes, Human, Pair 21 ; Disease Models, Animal ; Down Syndrome/drug therapy ; Down Syndrome/genetics ; Gene Expression Regulation ; Humans ; Mice ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/physiology ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/physiology ; Dyrk Kinases
Chemical Substances	Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2009-08-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-009-0123-2
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