PICK1–ICA69 Heteromeric BAR Domain Complex Regulates Synaptic Targeting and Surface Expression of AMPA Receptors

Cao, Mei; Xu, Junyu; Shen, Chong; Kam, Chuen; Huganir, Richard L.; Xia, Jun

doi:10.1523/jneurosci.2040-07.2007

Cited by 70 publications

(133 citation statements)

References 30 publications

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“…This interaction is important for the localization and stabilization of GluA1/GluA2 AMPA receptors to the synaptic area (Cai et al, 2006;Rumbaugh et al, 2003). Protein interacting with C kinase 1 (PICK1) links to the PDZ-binding domain of GluA2 and has a role in the clustering of the subunit and tethering of the receptor to the post-synaptic density and plasma membrane (Cao et al, 2007;Jin et al, 2006;Pan et al, 2007). Stargazin also has a role in the trafficking and localization of AMPA receptors at the cell surface, participating in the lateralization of AMPA receptors from extrasynaptic membrane to the synapse (Bats et al, 2007;Bedoukian et al, 2006;Chen et al, 2000).…”

Section: Ampa Subtype Of Glutamate Receptor Traffickingmentioning

confidence: 99%

Postmortem Brain: An Underutilized Substrate for Studying Severe Mental Illness

McCullumsmith

Hammond

Shan

et al. 2013

Neuropsychopharmacol

106

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We propose that postmortem tissue is an underutilized substrate that may be used to translate genetic and/or preclinical studies, particularly for neuropsychiatric illnesses with complex etiologies. Postmortem brain tissues from subjects with schizophrenia have been extensively studied, and thus serve as a useful vehicle for illustrating the challenges associated with this biological substrate. Schizophrenia is likely caused by a combination of genetic risk and environmental factors that combine to create a disease phenotype that is typically not apparent until late adolescence. The complexity of this illness creates challenges for hypothesis testing aimed at understanding the pathophysiology of the illness, as postmortem brain tissues collected from individuals with schizophrenia reflect neuroplastic changes from a lifetime of severe mental illness, as well as treatment with antipsychotic medications. While there are significant challenges with studying postmortem brain, such as the postmortem interval, it confers a translational element that is difficult to recapitulate in animal models. On the other hand, data derived from animal models typically provide specific mechanistic and behavioral measures that cannot be generated using human subjects. Convergence of these two approaches has led to important insights for understanding molecular deficits and their causes in this illness. In this review, we discuss the problem of schizophrenia, review the common challenges related to postmortem studies, discuss the application of biochemical approaches to this substrate, and present examples of postmortem schizophrenia studies that illustrate the role of the postmortem approach for generating important new leads for understanding the pathophysiology of severe mental illness.

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Section: Ampa Subtype Of Glutamate Receptor Traffickingmentioning

confidence: 99%

Postmortem Brain: An Underutilized Substrate for Studying Severe Mental Illness

McCullumsmith

Hammond

Shan

et al. 2013

Neuropsychopharmacol

106

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“…For instance, the small Arfaptin-related protein islet cell autoantigen of 69 kDa (ICA69, also known as ICA1) (Fig. 2) has been shown to associate with the BAR domain protein PICK1 and to inhibit its functions in AMPA receptor trafficking and synaptic plasticity (Cao et al, 2007). More than 75% of all ICA69 and PICK1 molecules have been reported to associate with each other in the brain; however, these inhibitory complexes only occurred in the cell body and dendrites (Cao et al, 2007;Wang et al, 2013).…”

Section: Acting As Suppressive Partnersmentioning

confidence: 99%

“…It is currently unclear whether ICA69-PICK binding reflects the formation of heterodimer BAR domain proteins or the heterooligomerization of homomeric BAR dimers. As dimers of BAR domain proteins are usually relatively stable and, moreover, the C-terminus of ICA69 might also be involved in the interaction (Cao et al, 2007), heterooligomerization and disruption of putative PICK1 oligomeric structures appears more likely.…”

Section: Acting As Suppressive Partnersmentioning

confidence: 99%

“…Finally, the functions of BAR domain proteins can be suppressed by tight association with another BAR domain protein, usually a superfamily member with a relatively simple domain organization. Recent work suggests that suppression of the function of BAR domain proteins by BAR-BAR heterooligomerization is an important molecular mechanisms that shapes the human brain (Cao et al, 2007;Charrier et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

Kessels

Qualmann

2015

Journal of Cell Science

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A plethora of cell biological processes involve modulations of cellular membranes. By using extended lipid-binding interfaces, some proteins have the power to shape membranes by attaching to them. Among such membrane shapers, the superfamily of Bin–Amphiphysin–Rvs (BAR) domain proteins has recently taken center stage. Extensive structural work on BAR domains has revealed a common curved fold that can serve as an extended membrane-binding interface to modulate membrane topologies and has allowed the grouping of the BAR domain superfamily into subfamilies with structurally slightly distinct BAR domain subtypes (N-BAR, BAR, F-BAR and I-BAR). Most BAR superfamily members are expressed in the mammalian nervous system. Neurons are elaborately shaped and highly compartmentalized cells. Therefore, analyses of synapse formation and of postsynaptic reorganization processes (synaptic plasticity) – a basis for learning and memory formation – has unveiled important physiological functions of BAR domain superfamily members. These recent advances, furthermore, have revealed that the functions of BAR domain proteins include different aspects. These functions are influenced by the often complex domain organization of BAR domain proteins. In this Commentary, we review these recent insights and propose to classify BAR domain protein functions into (1) membrane shaping, (2) physical integration, (3) action through signaling components, and (4) suppression of other BAR domain functions.

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“…PICK1 has recently been shown to bind to α7-nAChRs (Baer et al, 2007), and EphB2Rs are thought to bind PICK1 as well (Torres et al, 1998). PICK1 is usually not found concentrated at synapses, however, and in the case of AMPA receptors is thought to participate in trafficking both to and from the surface, rather than synaptic stabilization (Lu and Ziff, 2005;Cao et al, 2007). Nonetheless, the PDZ binding domains of EphB2Rs, as well as other binding motifs in the receptors, suggest numerous possible indirect links to α7-nAChRs.…”

Section: Discussionmentioning

confidence: 99%

EphB Receptors Co-Distribute with a Nicotinic Receptor Subtype and Regulate Nicotinic Downstream Signaling in Neurons

Liu¹,

Conroy²,

Stawicki³

et al. 2008

Molecular and Cellular Neuroscience

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Activation of nicotinic acetylcholine receptors (nAChRs) on neurons engages calcium-dependent signaling pathways regulating numerous events. Receptors containing α7 subunits (α7-nAChRs) are prominent in this because of their abundance and high relative calcium permeability. We show here that EphB2 receptors are co-localized with postsynaptic α7-nAChRs on chick ciliary ganglion neurons and that treatment of the cells with an ephrinB1 construct to activate the EphB receptors exerts physical restraints on both classes of receptors, diminishing their dispersal after spine retraction or lipid raft disruption. Moreover, the ephrinB1/EphB receptor complex specifically enhances the ability of α7-nAChRs to activate the transcription factor CREB, acting through a pathway including a receptor tyrosine kinase, a Src family member, PI3 kinase, and protein kinase A most distally. The enhancement does not appear to result from a change in the α7-nAChR current amplitude, suggesting a downstream target. The results demonstrate a role for ephrin/EphB action in nicotinic signaling.

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PICK1–ICA69 Heteromeric BAR Domain Complex Regulates Synaptic Targeting and Surface Expression of AMPA Receptors

Cited by 70 publications

References 30 publications

Postmortem Brain: An Underutilized Substrate for Studying Severe Mental Illness

Postmortem Brain: An Underutilized Substrate for Studying Severe Mental Illness

Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses

EphB Receptors Co-Distribute with a Nicotinic Receptor Subtype and Regulate Nicotinic Downstream Signaling in Neurons

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