The Cystic Fibrosis Transmembrane Conductance Regulator's Expanding SNARE Interactome

Tang, Bor Luen; Gee, Heon Yung; Lee, Min Goo

doi:10.1111/j.1600-0854.2011.01161.x

Cited by 31 publications

(20 citation statements)

References 78 publications

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“…The actin cytoskeleton modulates CFTR by multiple mechanisms including trafficking, gating, and assembly into signaling complexes. CFTR, like Ano1, also interacts with SNARES (syntaxins 1A, -3, -6, -7, -8, -16, and VAMP8) (44), which play a role in CFTR trafficking.…”

Section: Discussionmentioning

confidence: 99%

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Pérez‐Cornejo

Gokhale

Duran

et al. 2012

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

114

139

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The newly discovered Ca 2+ -activated Cl − channel (CaCC), Anoctamin 1 (Ano1 or TMEM16A), has been implicated in vital physiological functions including epithelial fluid secretion, gut motility, and smooth muscle tone. Overexpression of Ano1 in HEK cells or Xenopus oocytes is sufficient to generate Ca 2+ -activated Cl − currents, but the details of channel composition and the regulatory factors that control channel biology are incompletely understood. We used a highly sensitive quantitative SILAC proteomics approach to obtain insights into stoichiometric protein networks associated with the Ano1 channel. These studies provide a comprehensive footprint of putative Ano1 regulatory networks. We find that Ano1 associates with the signaling/scaffolding proteins ezrin, radixin, moesin, and RhoA, which link the plasma membrane to the cytoskeleton with very high stoichiometry. Ano1, ezrin, and moesin/radixin colocalize apically in salivary gland epithelial cells, and overexpression of moesin and Ano1 in HEK cells alters the subcellular localization of both proteins. Moreover, interfering RNA for moesin modifies Ano1 current without affecting its surface expression level. Another network associated with Ano1 includes the SNARE and SM proteins VAMP3, syntaxins 2 and -4, and syntaxin-binding proteins munc18b and munc18c, which are integral to translocation of vesicles to the plasma membrane. A number of other regulatory proteins, including GTPases, Ca 2+ -binding proteins, kinases, and lipid-interacting proteins are enriched in the Ano1 complex. These data provide stoichiometrically prioritized information about mechanisms regulating Ano1 function and trafficking to polarized domains of the plasma membrane.calcium | interactome | cross-linker | apical targeting

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Section: Discussionmentioning

confidence: 99%

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Pérez‐Cornejo

Gokhale

Duran

et al. 2012

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

114

139

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“…Syntaxin-1A also interacts with proteins of the ABCCx gene family, including CFTR (ABCC7), SUR1 (ABCC8), and SUR2 (ABCC9) (252,421,634). Syntaxin-1A regulates both the trafficking and gating of CTFR (791). By binding to the intracellular nucleotide binding folds of SUR1 and SUR2, syntaxin-1A negatively regulates K ATP channels (104, 421,634).…”

Section: Membrane Delivery and Anchoringmentioning

confidence: 99%

K_ATPChannels in the Cardiovascular System

Foster

Coetzee

2016

Physiological Reviews

193

237

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KATP channels are integral to the functions of many cells and tissues. The use of electrophysiological methods has allowed for a detailed characterization of KATP channels in terms of their biophysical properties, nucleotide sensitivities, and modification by pharmacological compounds. However, even though they were first described almost 25 years ago (Noma 1983, Trube and Hescheler 1984), the physiological and pathophysiological roles of these channels, and their regulation by complex biological systems, are only now emerging for many tissues. Even in tissues where their roles have been best defined, there are still many unanswered questions. This review aims to summarize the properties, molecular composition, and pharmacology of KATP channels in various cardiovascular components (atria, specialized conduction system, ventricles, smooth muscle, endothelium, and mitochondria). We will summarize the lessons learned from available genetic mouse models and address the known roles of KATP channels in cardiovascular pathologies and how genetic variation in KATP channel genes contribute to human disease.

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“…3A) (Springer and Schekman 1998;Aridor et al 1999;Mettlen et al 2010). This is evident in, for example, the sequential CTF-based TRaCKS transiently engaged by the cystic fibrosis transmembrane conductance regulator (CTFR) to provide a precise trajectory for its trafficking from the ER to the plasma membrane (Tang et al 2011a), a process that is disrupted in disease ). As might be expected, CFTR TRaCKS biology is different from the sequential TRaCKS generated by glycosylation enzymes to generate Golgi compartments (see below).…”

Section: Proteostasis By Membrane Traffickingmentioning

confidence: 99%

Expanding Proteostasis by Membrane Trafficking Networks

Hutt

Balch

2013

Cold Spring Harbor Perspectives in Biology

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The folding biology common to all three kingdoms of life (Archaea, Bacteria, and Eukarya) is proteostasis. The proteostasis network (PN) functions as a "cloud" to generate, protect, and degrade the proteome. Whereas microbes (Bacteria, Archaea) have a single compartment, Eukarya have numerous subcellular compartments. We examine evidence that Eukarya compartments use coat, tether, and fusion (CTF) membrane trafficking components to form an evolutionarily advanced arm of the PN that we refer to as the "trafficking PN" (TPN). We suggest that the TPN builds compartments by generating a mosaic of integrated cargo-specific trafficking signatures (TRaCKS). TRaCKS control the temporal and spatial features of protein-folding biology based on the Anfinsen principle that the local environment plays a critical role in managing protein structure. TPN-generated endomembrane compartments apply a "quinary" level of structural control to modify the secondary, tertiary, and quaternary structures defined by the primary polypeptide-chain sequence. The development of Anfinsen compartments provides a unifying foundation for understanding the purpose of endomembrane biology and its capacity to drive extant Eukarya function and diversity.

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The Cystic Fibrosis Transmembrane Conductance Regulator's Expanding SNARE Interactome

Cited by 31 publications

References 78 publications

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

K_ATPChannels in the Cardiovascular System

Expanding Proteostasis by Membrane Trafficking Networks

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The Cystic Fibrosis Transmembrane Conductance Regulator's Expanding SNARE Interactome

Cited by 31 publications

References 78 publications

Anoctamin 1 (Tmem16A) Ca 2 + -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Anoctamin 1 (Tmem16A) Ca 2 + -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

KATPChannels in the Cardiovascular System

Expanding Proteostasis by Membrane Trafficking Networks

Contact Info

Product

Resources

About

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

K_ATPChannels in the Cardiovascular System