The protein kinase Cα binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits

Dev, Kumlesh K.; Nishimune, Atsushi; Henley, Jeremy M.; Nakanishi, Shigetada

doi:10.1016/s0028-3908(98)00230-5

Cited by 195 publications

(215 citation statements)

References 26 publications

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“…It has since been shown to bind numerous transmembrane receptors, transporters, and ion channels via its single N-terminal PDZ domain (Madsen et al, 2005). In contrast to most PDZ proteins, it is capable of interacting with both class I and class II PDZ ligands, as well as with various atypical motifs (Staudinger et al, 1997;Dev et al, 1999;Madsen et al, 2005). PICK1 also contains a coiled-coil motif that has been proposed to form a BAR (Bin/amphiphysin/Rvs.)…”

Section: Discussionmentioning

confidence: 99%

“…We reported previously that the PDZ protein CASK binds to parkin via this C-terminal motif (Fallon et al, 2002). As proteins with PDZ-binding motifs often interact with several distinct PDZ proteins (Srivastava et al, 1998;Dev et al, 1999), we used a candidate approach to identify additional PDZ proteins that interact with the Cterminus of parkin. We carried out pulldowns from mouse brain synaptosomes using GST fused to various parkin do- mains ( Figure 1A).…”

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confidence: 99%

“…This mutation is particularly interesting because it truncates only the last 13 amino acids of parkin, eliminating its PDZ-binding motif, but leaves the critical E2-binding RING domain intact (Lucking et al, 2000;Zhang et al, 2000). Interestingly, although CASK contains a wellcharacterized class II PDZ domain, the PDZ domain of PICK1 can interact with both type I and type II as well as with atypical PDZ ligands (Staudinger et al, 1997;Dev et al, 1999;Williams et al, 2003;Madsen et al, 2005). In contrast, both PSD95 and Veli-1 contain distinct type I PDZ domains and, accordingly, these do not bind to the GST-IR WT construct.…”

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confidence: 99%

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Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Joch

Ase

Chen

et al. 2007

MBoC

126

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Mutations in the parkin gene result in an autosomal recessive juvenile-onset form of Parkinson's disease. As an E3 ubiquitin-ligase, parkin promotes the attachment of ubiquitin onto specific substrate proteins. Defects in the ubiquitination of parkin substrates are therefore believed to lead to neurodegeneration in Parkinson's disease. Here, we identify the PSD-95/Discs-large/Zona Occludens-1 (PDZ) protein PICK1 as a novel parkin substrate. We find that parkin binds PICK1 via a PDZ-mediated interaction, which predominantly promotes PICK1 monoubiquitination rather than polyubiquitination. Consistent with monoubiquitination and recent work implicating parkin in proteasome-independent pathways, parkin does not promote PICK1 degradation. However, parkin regulates the effects of PICK1 on one of its other PDZ partners, the acid-sensing ion channel (ASIC). Overexpression of wild-type, but not PDZ binding-or E3 ubiquitinligase-defective parkin abolishes the previously described, protein kinase C-induced, PICK1-dependent potentiation of ASIC2a currents in non-neuronal cells. Conversely, the loss of parkin in hippocampal neurons from parkin knockout mice unmasks prominent potentiation of native ASIC currents, which is normally suppressed by endogenous parkin in wild-type neurons. Given that ASIC channels contribute to excitotoxicity, our work provides a mechanism explaining how defects in parkin-mediated PICK1 monoubiquitination could enhance ASIC activity and thereby promote neurodegeneration in Parkinson's disease. INTRODUCTIONParkinson's disease (PD) is characterized by the selective and progressive loss of midbrain dopamine neurons resulting in motor dysfunction and disability. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism, which accounts for a large proportion of genetically linked PD cases (Kitada et al., 1998). Parkin encodes a 465-amino acid protein (ϳ52 kDa) that is expressed in multiple tissues and functions in the ubiquitin (Ub) system as an E3 Ub-ligase (Shimura et al., 2000). Ubiquitination of substrate proteins is a tightly regulated process, requiring the combined activity of three enzymes: an E1 Ub-activating enzyme, E2 Ub-conjugating enzymes, and E3 Ub-ligases (Hershko and Ciechanover, 1998). E3 Ub-ligases bind substrate proteins and therefore regulate and confer specificity to the ubiquitination reaction. Typically, ubiquitination leads to the assembly of a K48-linked polyubiquitin chain on the substrate, which targets it for degradation by the 26S proteasome, a large multimeric proteolytic complex (Voges et al., 1999). Accordingly, defects in parkin-mediated ubiquitination have been proposed to result in the failure to target parkin substrates to the proteasome for degradation (Kahle et al., 2000;Feany and Pallanck, 2003;Giasson and Lee, 2003). The ensuing accumulation of parkin substrates is believed, in turn, to induce the cellular toxicity and dopamine neuron loss seen in PD. Although numerous parkin substrates have been identified (Zhang et al., 2000;Chung et al., 2001...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Joch

Ase

Chen

et al. 2007

MBoC

126

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“…particular postsynaptic roles. For example, Pick 1 and GRIP1, which both interact with the C-terminal terminal of the AMPA receptor subunits, GluR2/3, are involved in their internalization and synaptic stabilization (Dong et al 1999;Dev et al 1999;Chung et al 2000;Daw et al 2000;El-Husseini et al 2000;Osten et al 2000). SAP97 interacts with the AMPA receptor subunit GluR1 and stabilizes receptor protein expression at postsynaptic sites (Leonard et al 1998;Jourdi et al 2001;Sans et al 2001).…”

Section: Discussionmentioning

confidence: 99%

Selective reduction of a PDZ protein, SAP‐97, in the prefrontal cortex of patients with chronic schizophrenia

Toyooka

Iritani

Makifuchi

et al. 2002

Journal of Neurochemistry

111

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Many postsynaptic density proteins carrying postsynaptic density-95/discs large/zone occludens-1 (PDZ) domain(s) interact with glutamate receptors to control receptor dynamics and synaptic plasticity. Here we examined the expression of PDZ proteins, synapse-associated protein (SAP) 97, postsynaptic density (PSD)-95, chapsyn-110, GRIP1 and SAP102, in post-mortem brains of schizophrenic patients and control subjects, and evaluated their contribution to schizophrenic pathology. Among these PDZ proteins, SAP97 exhibited the most marked change: SAP97 protein levels were decreased to less than half that of the control levels specifically in the prefrontal cortex of schizophrenic patients. In parallel, its binding partner, GluR1, similarly decreased in the same brain region. The correlation between SAP97 and GluR1 levels in control subjects was, however, altered in schizophrenic patients. SAP102 levels were also significantly reduced in the hippocampus of schizophrenic patients, but this reduction was correlated with sample storage time and post-mortem interval. There were no changes in the levels of the other PDZ proteins in any of the regions examined. In addition, neuroleptic treatment failed to mimic the SAP97 change. These findings suggest that a phenotypic loss of SAP97 is associated with the postsynaptic impairment in prefrontal excitatory circuits of schizophrenic patients. Keywords: chapsyn-110, GRIP1, PSD-95, psychosis, SAP102, SAP97. Address correspondence and reprint requests to Hiroyuki Nawa, Department of Molecular Biology, Brain Research Institute, Niigata University, Asahimachi-dori 1-757, Niigata 951-8585, Japan. E-mail: hnawa@bri.niigata-u.ac.jpAbbreviations used: ABP, AMPA receptor-binding protein; AMPA, a-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid; BDNF, brainderived neurotrophic factor; DTT, dithiothreitol; LPT, long-term potentiation; NSE, neuron-specific enolase; PAGE, polyacrylamide gel electrophoresis; PDZ, PSD-95/discs large/zone occludens-1; PVDF, polyvinylidene difluoride; PSD, postsynaptic density; SAP, synapseassociated protein; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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“…GRIP (Dong et al, 1997), AMPA receptor-binding protein (ABP), also known as GRIP2 , and PICK1 (Dev et al, 1999;Xia et al, 1999) can interact with the PDZ ligand at the extreme C-terminus of GluR2 and GluR3 (Fig. 1B) (Sheng and Sala, 2001).…”

Section: Ampar Traffic Ampar Biosynthesis and Ampar Interaction Partnersmentioning

confidence: 99%

Regulation of AMPA receptors and synaptic plasticity

et al. 2009

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The protein kinase Cα binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits

Cited by 195 publications

References 26 publications

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Parkin-mediated Monoubiquitination of the PDZ Protein PICK1 Regulates the Activity of Acid-sensing Ion Channels

Selective reduction of a PDZ protein, SAP‐97, in the prefrontal cortex of patients with chronic schizophrenia

Regulation of AMPA receptors and synaptic plasticity

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