Coxsackievirus and adenovirus receptor (CAR) mediates trafficking of acid sensing ion channel 3 (ASIC3) via PSD-95

Excoffon, Katherine J. D. A.; Kolawole, Abimbola O.; Kusama, Nobuyoshi; Gansemer, Nicholas D.; Sharma, Priyanka; Hruska-Hageman, Alesia M.; Petroff, Elena; Benson, Christopher J.

doi:10.1016/j.bbrc.2012.07.033

Cited by 7 publications

(5 citation statements)

References 29 publications

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“…CAR is a virus receptor that mediates adenovirus and coxsackievirus infection. CAR is also a critical cell adhesion protein that plays a role in the junctional localization of important scaffolding proteins and cognate signaling proteins, such as PSD-95 and ASIC3 (Excoffon, Kolawole et al 2012). Moreover, the essential nature of CAR may be due to its ability to traffic or modulate the junctional stability of important proteins, such as MAGI-1, connexin 45, β-catenin, and ZO-1, particularly at cell junctions and the cardiac intercalated disc (Lim, Xiong et al 2008, Pazirandeh, Sultana et al 2011, Freiberg, Sauter et al 2014).…”

Section: Discussionmentioning

confidence: 99%

The PDZ3 domain of the cellular scaffolding protein MAGI-1 interacts with the Coxsackievirus and adenovirus receptor (CAR)

Yan

Sharma

Kolawole

et al. 2015

The International Journal of Biochemistry & Cell Biology

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The Coxsackievirus and adenovirus receptor (CAR) is an essential cellular protein that is involved in cell-cell adhesion, protein trafficking, and viral infection. The major isoform of CAR is selectively sorted to the basolateral membrane of polarized epithelial cells where it co-localizes with the cellular scaffolding protein membrane-associated guanylate kinase with inverted domain structure-1 (MAGI-1). Previously, we demonstrated CAR interacts with MAGI-1 through a PDZ–domain dependent interaction. Here, we show that the PDZ3 domain of MAGI-1 is exclusively responsible for the high affinity interaction between the seven exon isoform of CAR and MAGI-1 using yeast-two-hybrid analysis and confirming this interaction biochemically and in cellular lysates by in vitro pull down assay and co-immunoprecipitation. The high affinity interaction between the PDZ3 domain and CAR C-terminus was measured by fluorescence resonance energy transfer. Further, we investigated the biological relevance of this high affinity interaction between CAR and the PDZ3 domain of MAGI-1 and found that it does not alter CAR-mediated adenovirus infection. By contrast, interruption of this high affinity interaction altered the localization of MAGI-1 indicating that CAR is able to traffic MAGI-1 to cell junctions. These data deepen the molecular understanding of the interaction between CAR and MAGI-1 and indicate that although CAR plays a role in trafficking PDZ-based scaffolding proteins to cellular junctions, association with a high affinity intracellular binding partner does not significantly alter adenovirus binding and entry via CAR.

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Section: Discussionmentioning

confidence: 99%

The PDZ3 domain of the cellular scaffolding protein MAGI-1 interacts with the Coxsackievirus and adenovirus receptor (CAR)

Yan

Sharma

Kolawole

et al. 2015

The International Journal of Biochemistry & Cell Biology

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“…In growth cones CAR seems to associate with actin filaments to modulate the cytoskeletal organization during growth and migration (Huang et al, 2007). Furthermore, CAR is able to affect the trafficking of E-cadherin and ASIC3, a H + -gated cation channel implicated in mechanosensation (Excoffon et al, 2012). E-cadherin trafficking is dependent on phosphorylation of CAR and may serve to stabilize cell-cell adhesion in human epithelial cells (Hussain et al, 2011;Morton et al, 2013).…”

Section: Extra-and Intracellular Molecular Interactions Of Carmentioning

confidence: 99%

Cell-cell communication mediated by the CAR subgroup of immunoglobulin cell adhesion molecules in health and disease

Matthäus

Langhorst

Schütz

et al. 2017

Molecular and Cellular Neuroscience

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The immunoglobulin superfamily represents a diverse set of cell-cell contact proteins and includes well-studied members such as NCAM1, DSCAM, L1 or the contactins which are strongly expressed in the nervous system. In this review we put our focus on the biological function of a less understood subgroup of Ig-like proteins composed of CAR (coxsackievirus and adenovirus receptor), CLMP (CAR-like membrane protein) and BT-IgSF (brain and testis specific immunoglobulin superfamily). The CAR-related proteins are type I transmembrane proteins containing an N-terminal variable (V-type) and a membrane proximal constant (C2-type) Ig domain in their extracellular region which are implicated in homotypic adhesion. They are highly expressed during embryonic development in a variety of tissues including the nervous system whereby in adult stages the protein level of CAR and CLMP decreases, only BT-IgSF expression increases within age. CAR-related proteins are concentrated at specialized cell-cell communication sites such as gap or tight junctions and are present at the plasma membrane in larger protein complexes. Considerable progress has been made on the molecular structure and interactions of CAR while research on CLMP and BT-IgSF is at an early stage. Studies on mouse mutants revealed biological functions of CAR in the heart and for CLMP in the gastrointestinal and urogenital systems. Furthermore, CAR and BT-IgSF appear to regulate synaptic function in the hippocampus.

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“…Co‐expression of ASIC3 and MAGI‐1 results in a decrease in both ASIC3 membrane level as well as proton‐evoked currents in peripheral neurons. Interestingly, coexpression of CAR Ex7 can result in a tripartite interaction that re‐establishes trafficking of ASIC3 to the cell surface (Excoffon et al., 2012). This demonstrates the importance of MAGI‐1, acting as a linker, to modulate membrane protein trafficking, localization, and signaling.…”

Section: Introductionmentioning

confidence: 99%

The magic of MAGI‐1: A scaffolding protein with multi signalosomes and functional plasticity

Excoffon

Avila

Alghamri

et al. 2022

Biology of the Cell

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MAGI-1 is a critical cellular scaffolding protein with over 110 different cellular and microbial protein interactors. Since the discovery of MAGI-1 in 1997, MAGI-1 has been implicated in diverse cellular functions such as polarity, cell-cell communication, neurological processes, kidney function, and a host of diseases including cancer and microbial infection. Additionally, MAGI-1 has undergone nomenclature changes in response to the discovery of an additional PDZ domain, leading to lack of continuity in the literature. We address the nomenclature of MAGI-1 as well as summarize many of the critical functions of the known interactions. Given the importance of many of the interactors, such as human papillomavirus E6, the Coxsackievirus and adenovirus receptor (CAR), and PTEN, the enhancement or disruption of MAGI-based interactions has the potential to affect cellular functions that can potentially be harnessed as a therapeutic strategy for a variety of diseases.

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Coxsackievirus and adenovirus receptor (CAR) mediates trafficking of acid sensing ion channel 3 (ASIC3) via PSD-95

Cited by 7 publications

References 29 publications

The PDZ3 domain of the cellular scaffolding protein MAGI-1 interacts with the Coxsackievirus and adenovirus receptor (CAR)

The PDZ3 domain of the cellular scaffolding protein MAGI-1 interacts with the Coxsackievirus and adenovirus receptor (CAR)

Cell-cell communication mediated by the CAR subgroup of immunoglobulin cell adhesion molecules in health and disease

The magic of MAGI‐1: A scaffolding protein with multi signalosomes and functional plasticity

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