Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)

Hruska-Hageman, Alesia M.; Wemmie, John A.; Price, Margaret P.; Welsh, Michael J.

doi:10.1042/0264-6021:3610443

Cited by 90 publications

(130 citation statements)

References 48 publications

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“…Indeed, PICK1 is known to target the activated form of PKC␣ to several transmembrane proteins for phosphorylation in a PDZ-dependent manner, which, in turn, alters their trafficking and functional regulation (Xia et al, 1999;Baron et al, 2002a;Williams et al, 2003). For instance, PICK1 binds to the C-termini of several isoforms of the ASIC family of proton-gated ion channels (ASIC1a, 2a, and 2b) via its PDZ domain (Duggan et al, 2002;Hruska-Hageman et al, 2002). Further, PICK1 is believed to target activated PKC␣ to ASIC2a, thereby leading to the phosphorylation of the channel in its cytoplasmic tail and to the potentiation of ASIC2a currents (Baron et al, 2002a).…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, PICK1 can dimerize via its central coiled-coil motif and thereby promote protein complex formation between its binding partners. One such PICK1-associated protein is the proton-gated ion channel ASIC2a, a mammalian member of the degenerin/epithelial Na ϩ channel (DEG/ ENaC) superfamily (Duggan et al, 2002;Hruska-Hageman et al, 2002). Interestingly, Baron et al (2002a) reported that activation of PKC strongly potentiates ASIC2a currents in a PICK1-dependent manner.…”

Section: Parkin Suppresses Pick1-mediated Potentiation Of Asic2a Currmentioning

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

127

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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%

Section: Parkin Suppresses Pick1-mediated Potentiation Of Asic2a Currmentioning

confidence: 99%

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

Joch

Ase

Chen

et al. 2007

MBoC

127

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“…ASIC1a has similar function in both cell types (10). For measurements of [Ca 2ϩ ] c , COS-7 cells were transfected by electroporation (26) and plated on collagen-coated glass cover slips. For patch-clamp studies and measurements of lactate dehydrogenase (LDH) release, Chinese hamster ovary cells, and COS-7 cells, respectively, were transfected with TransFast Lipid Reagent (Promega) and cultured on 35-mm Petri dishes.…”

Section: Methodsmentioning

confidence: 99%

Extracellular acidosis increases neuronal cell calcium by activating acid-sensing ion channel 1a

Yermolaieva

Leonard

Schnizler

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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345

386

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“…In particular there has been a lot of interest in PICK1 since it was originally identified as an interactor for PKCa (Staudinger et al 1995(Staudinger et al , 1997. In addition, to PKCa and GluR2, PICK1 also interacts with a number of other proteins including mGluR7 (Boudin et al 2000;Dev et al 2000;El Far et al 2000), non-voltage-gated Na 1 channels (Baron et al 2002;Duggan et al 2002;Hruska-Hageman et al 2002) and ephrin receptors (Torres et al 1998). Although PICK1 contains only a single PDZ domain, it can also dimerize via a coiled-coil domain (Perez et al 2001) providing the possibility that PICK1 dimers could target other proteins such as PKCa to AMPARs.…”

Section: The Pdz Sitementioning

confidence: 99%

GluR2 protein-protein interactions and the regulation of AMPA receptors during synaptic plasticity

Duprat

Daw

Lim

et al. 2003

Phil. Trans. R. Soc. Lond. B

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AMPA-type glutamate receptors mediate most fast excitatory synaptic transmissions in the mammalian brain. They are critically involved in the expression of long-term potentiation and long-term depression, forms of synaptic plasticity that are thought to underlie learning and memory. A number of synaptic proteins have been identified that interact with the intracellular C-termini of AMPA receptor subunits. Here, we review recent studies and present new experimental data on the roles of these interacting proteins in regulating the AMPA receptor function during basal synaptic transmission and plasticity.

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Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)

Cited by 90 publications

References 48 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

Extracellular acidosis increases neuronal cell calcium by activating acid-sensing ion channel 1a

GluR2 protein-protein interactions and the regulation of AMPA receptors during synaptic plasticity

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