<scp>CNIH4</scp> Interacts with Newly Synthesized <scp>GPCR</scp> and Controls Their Export from the Endoplasmic Reticulum

Sauvageau, Étienne; Rochdi, Moulay Driss; Oueslati, Morad; Hamdan, Fadi F.; Percherancier, Yann; Simpson, Jeremy C.; Pepperkok, Rainer; Bouvier, Michel

doi:10.1111/tra.12148

Cited by 53 publications

(53 citation statements)

References 61 publications

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“…Among four CNI homologs (CNIHs) in mammals, CNIH2 and CNIH3 function as α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors for glutamatergic neurotransmission in the central nervous system (Herring et al, 2013;Jackson and Nicoll, 2009;Schwenk et al, 2009). CNIH4 interacts with both G-protein-coupled receptors (GPCRs) and Sec23 and Sec24 and, thus, acts as a cargo receptor for recruiting GPCRs into COPII vesicles and transporting them to the cell surface (Sauvageau et al, 2014). Additionally, human CNIs functionally complement the loss of Erv14 in yeast (Castro et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

Fuchs

Zhang

et al. 2016

Journal of Cell Science

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Positive-strand RNA viruses invariably assemble their viral replication complexes (VRCs) by remodeling host intracellular membranes. How viral replication proteins are targeted to specific organelle membranes to initiate VRC assembly remains elusive. Brome mosaic virus (BMV), whose replication can be recapitulated in Saccharomyces cerevisiae, assembles its VRCs by invaginating the outer perinuclear endoplasmic reticulum (ER) membrane. Remarkably, BMV replication protein 1a (BMV 1a) is the only viral protein required for such membrane remodeling. We show that ER-vesicle protein of 14 kD (Erv14), a cargo receptor of coat protein complex II (COPII), interacts with BMV 1a. Moreover, the perinuclear ER localization of BMV 1a is disrupted in cells lacking ERV14 or expressing dysfunctional COPII coat components (Sec13, Sec24 or Sec31). The requirement of Erv14 for the localization of BMV 1a is bypassed by addition of a Sec24-recognizable sorting signal to BMV 1a or by overexpressing Sec24, suggesting a coordinated effort by both Erv14 and Sec24 for the proper localization of BMV 1a. The COPII pathway is well known for being involved in protein secretion; our data suggest that a subset of COPII coat proteins have an unrecognized role in targeting proteins to the perinuclear ER membrane.

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Section: Discussionmentioning

confidence: 99%

An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

Fuchs

Zhang

et al. 2016

Journal of Cell Science

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“…Moreover, TARPs are essential for ER export of correctly assembled receptors 85 and remain part of the AMPAR complex throughout Golgi processing and forward trafficking to eventual surface expression at the postsynaptic density 86 . Similarly, cornichons have a welldefined role in the export of specific proteins from the ER 87,88 including AMPARs 89,90 .…”

Section: Rna Editing Ampar Assembly and Er Exitmentioning

confidence: 99%

Synaptic AMPA receptor composition in development, plasticity and disease

2016

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General rightsThis document is made available in accordance with publisher policies. Please cite only the published version using the reference above. PrefaceAMPARs are assemblies of four core subunits, GluA1-4, that mediate most fast excitatory neurotransmission. The component subunits determine the functional properties of AMPARs and the prevailing view is that the subunit composition also determines AMPAR trafficking, which is dynamically regulated during development, synaptic plasticity, and in response to neuronal stress in disease. Recently, the subunit-dependence of AMPAR trafficking has been questioned leading to a reappraisal of the field. Here we review what is known, uncertain, conjectured and unknown about the roles of individual subunits and how they impact on AMPAR assembly, trafficking and function under normal and pathological conditions. IntroductionAMPA receptors (AMPARs) are a subtype of ionotropic glutamate receptors that are the 'work-horses' of fast excitatory neurotransmission in the CNS. Developmentallyand activity-regulated changes in the numbers and properties of AMPARs localized at the postsynaptic membrane are essential for excitatory synapse formation, stabilization, synaptic plasticity and neural circuit formation. Consequently, the logistics of the delivery, retention and removal of individual AMPARs with defined subunit compositions at specific synapses is highly complex. A typical cortical or hippocampal pyramidal neuron contains on the order of 10,000 synapses and the AMPARs at each synapse are independently and dynamically regulated in response to developmental cues, synaptic activity and environmental stresses. Furthermore, defects in the processes that control AMPAR assembly, trafficking and synaptic expression are intimately linked to psychiatric and neurological conditions, and also with cognitive decline in neurodegenerative diseases. Remarkable progress has been achieved in understanding how AMPAR trafficking, is orchestrated by a large array of AMPAR interacting proteins. These studies have established a set of hierarchical subunit-specific rules that control AMPAR trafficking under basal and activity-dependent conditions. Furthermore, there has been a growing appreciation that subunit composition can tune the properties of AMPARs to specific conditions. Nonetheless, how AMPARs comprising different subunits are differentially trafficked to control synaptic development, stabilisation and plasticity is a key unanswered question. Here, we provide an overview of the current state of knowledge of subunit-specific AMPAR trafficking and outline what we believe to be the key unresolved questions in the field. 2 Subunit-specific traffickingMost AMPARs are heterotetrameric assemblies of combinations of the subunits GluA1, GluA2, GluA3 and GluA4. AMPARs are expressed in both neurons and glia throughout the CNS 1 and have a turnover time of between 10 hours and 2 days depending on the type of neuron and developmental stage 2,3 . Each subunit has an identical membrane topology and c...

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“…To date, several integral membrane cargo, including TGFα, AMPA receptors, and G protein-coupled receptors (GPCRs), are known to depend on Cornichon function for efficient delivery (Bokel et al 2006, Sauvageau et al 2014, Schwenk et al 2009). Systematic studies in yeast have identified more than 30 transmembrane cargo proteins that accumulate in the ER when cells are deleted for Erv14 (Herzig et al 2012, Pagant et al 2015.…”

Section: Cornichon Proteinsmentioning

confidence: 99%

“…Regulation can be coupled to signaling pathways. In addition to the role of SCAP and iRhom2 discussed, a well-studied example of regulation is provided by GPCRs, for which many membrane-associated and cytosolic effector molecules that regulate ER-to-Golgi traffic have been identified (Achour et al 2008, Dong et al 2007, Sauvageau et al 2014. One such effector is Rab acceptor family 2 (PARF2), a protein that serves as a gatekeeper in the ER for the GB1 subunit of the GABA B receptor (Doly et al 2015).…”

Section: Fine-tuning Of Protein Deploymentmentioning

confidence: 99%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

175

191

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Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.

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CNIH4 Interacts with Newly Synthesized GPCR and Controls Their Export from the Endoplasmic Reticulum

Cited by 53 publications

References 61 publications

An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER

Synaptic AMPA receptor composition in development, plasticity and disease

Cargo Capture and Bulk Flow in the Early Secretory Pathway

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