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CKAMP44

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https://www.readbyqxmd.com/read/26932439/gsg1l-suppresses-ampa-receptor-mediated-synaptic-transmission-and-uniquely-modulates-ampa-receptor-kinetics-in-hippocampal-neurons
#1
Xinglong Gu, Xia Mao, Marc P Lussier, Mary Anne Hutchison, Liang Zhou, F Kent Hamra, Katherine W Roche, Wei Lu
Regulation of AMPA receptor (AMPAR)-mediated synaptic transmission is a key mechanism for synaptic plasticity. In the brain, AMPARs assemble with a number of auxiliary subunits, including TARPs, CNIHs and CKAMP44, which are important for AMPAR forward trafficking to synapses. Here we report that the membrane protein GSG1L negatively regulates AMPAR-mediated synaptic transmission. Overexpression of GSG1L strongly suppresses, and GSG1L knockout (KO) enhances, AMPAR-mediated synaptic transmission. GSG1L-dependent regulation of AMPAR synaptic transmission relies on the first extracellular loop domain and its carboxyl-terminus...
March 2, 2016: Nature Communications
https://www.readbyqxmd.com/read/26645823/facilitated-c-fos-induction-in-mice-deficient-for-the-ampa-receptor-associated-protein-ckamp44
#2
Boyi Yang, Christof Dormann, Miriam A Vogt, Rolf Sprengel, Peter Gass, Dragos Inta
The recently identified Cystine-knot containing AMPAR-associated protein (Ckamp44) represents a novel AMPAR-related protein that critically controls AMPAR-mediated currents and short-term plasticity. However, the effects of the lack of this protein at network level are not entirely understood. Here we used c-Fos brain mapping to analyse whether the excitatory/inhibitory balance is altered in the absence of the Ckamp44. We found that Ckamp44(-/-) mice treated with an NMDAR antagonist exhibited a very robust c-Fos expression pattern, similar with that seen in mice lacking the GluN2A subunit of NMDAR treated with the same compound...
October 2016: Cellular and Molecular Neurobiology
https://www.readbyqxmd.com/read/26623514/auxiliary-subunits-of-the-ckamp-family-differentially-modulate-ampa-receptor-properties
#3
Paul Farrow, Konstantin Khodosevich, Yechiam Sapir, Anton Schulmann, Muhammad Aslam, Yael Stern-Bach, Hannah Monyer, Jakob von Engelhardt
AMPA receptor (AMPAR) function is modulated by auxiliary subunits. Here, we report on three AMPAR interacting proteins-namely CKAMP39, CKAMP52 and CKAMP59-that, together with the previously characterized CKAMP44, constitute a novel family of auxiliary subunits distinct from other families of AMPAR interacting proteins. The new members of the CKAMP family display distinct regional and developmental expression profiles in the mouse brain. Notably, despite their structural similarities they exert diverse modulation on AMPAR gating by influencing deactivation, desensitization and recovery from desensitization, as well as glutamate and cyclothiazide potency to AMPARs...
December 1, 2015: ELife
https://www.readbyqxmd.com/read/26255765/advances-in-the-pharmacology-of-lgics-auxiliary-subunits
#4
REVIEW
Pablo Galaz, Rafael Barra, Hector Figueroa, Trinidad Mariqueo
Ligand-gated ion channels (LGICs) are cell surface integral proteins that mediate the fast neurotransmission in the nervous system. LGICs require auxiliary subunits for their trafficking, assembly and pharmacological modulation. Auxiliary subunits do not form functional homomeric receptors, but are reported to assemble with the principal subunits in order to modulate their pharmacological profiles. For example, nACh receptors are built at least by co-assemble of α and β subunits, and the neuronal auxiliary subunits β3 and α5 and muscle type β, δ, γ, and ϵ determine the agonist affinity of these receptors...
November 2015: Pharmacological Research: the Official Journal of the Italian Pharmacological Society
https://www.readbyqxmd.com/read/25110960/auxiliary-subunits-shepherding-ampa-receptors-to-the-plasma-membrane
#5
REVIEW
Simon C Haering, Daniel Tapken, Steffen Pahl, Michael Hollmann
Ionotropic glutamate receptors (iGluRs) are tetrameric ligand-gated cation channels that mediate excitatory signal transmission in the central nervous system (CNS) of vertebrates. The members of the iGluR subfamily of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptors (AMPARs) mediate most of the fast excitatory signal transmission, and their abundance in the postsynaptic membrane is a major determinant of the strength of excitatory synapses. Therefore, regulation of AMPAR trafficking to the postsynaptic membrane is an important constituent of mechanisms involved in learning and memory formation, such as long-term potentiation (LTP) and long-term depression (LTD)...
2014: Membranes
https://www.readbyqxmd.com/read/25066086/coexpressed-auxiliary-subunits-exhibit-distinct-modulatory-profiles-on-ampa-receptor-function
#6
Konstantin Khodosevich, Eric Jacobi, Paul Farrow, Anton Schulmann, Alexandru Rusu, Ling Zhang, Rolf Sprengel, Hannah Monyer, Jakob von Engelhardt
Gating properties and surface trafficking of AMPA receptors (AMPARs) are modulated by auxiliary subunits. Here we studied the function of coexpressed auxiliary subunits belonging to two different classes. We focused on TARP γ-8 and CKAMP44 in dentate gyrus (DG) granule cells, since both subunits are highly expressed in this cell type. TARP γ-8 and CKAMP44 decrease the rate of deactivation but have an opposing influence on receptor desensitization, which accounts for their differential modulation of synaptic short-term plasticity...
August 6, 2014: Neuron
https://www.readbyqxmd.com/read/24498314/c-terminal-interactors-of-the-ampa-receptor-auxiliary-subunit-shisa9
#7
Anna R Karataeva, Remco V Klaassen, Jasper Ströder, Marta Ruiperez-Alonso, Johannes J J Hjorth, Pim van Nierop, Sabine Spijker, Huibert D Mansvelder, August B Smit
Shisa9 (initially named CKAMP44) has been identified as auxiliary subunit of the AMPA-type glutamate receptors and was shown to modulate its physiological properties. Shisa9 is a type-I transmembrane protein and contains a C-terminal PDZ domain that potentially interacts with cytosolic proteins. In this study, we performed a yeast two-hybrid screening that yielded eight PDZ domain-containing interactors of Shisa9, which were independently validated. The identified interactors are known scaffolding proteins residing in the neuronal postsynaptic density...
2014: PloS One
https://www.readbyqxmd.com/read/23426437/auxiliary-subunits-provide-new-insights-into-regulation-of-ampa-receptor-trafficking
#8
REVIEW
Akio Sumioka
Glutamate is a major excitatory neurotransmitter in the vertebrate brain. Among the ionotropic glutamate receptors, α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate (AMPA) glutamate receptors are the major receptors mediating excitatory fast synaptic transmission. AMPA receptors are also responsible for modifying synaptic strength through the regulation of their numbers at synapses. Their high regulatability, therefore, could contribute to the mechanisms of synaptic plasticity. The mechanisms regulating AMPA receptor trafficking have evoked great interest through the decades...
April 2013: Journal of Biochemistry
https://www.readbyqxmd.com/read/22813734/differences-in-ampa-and-kainate-receptor-interactomes-facilitate-identification-of-ampa-receptor-auxiliary-subunit-gsg1l
#9
Natalie F Shanks, Jeffrey N Savas, Tomohiko Maruo, Ondrej Cais, Atsushi Hirao, Souichi Oe, Anirvan Ghosh, Yasuko Noda, Ingo H Greger, John R Yates, Terunaga Nakagawa
AMPA receptor (AMPA-R) complexes consist of channel-forming subunits, GluA1-4, and auxiliary proteins, including TARPs, CNIHs, synDIG1, and CKAMP44, which can modulate AMPA-R function in specific ways. The combinatorial effects of four GluA subunits binding to various auxiliary subunits amplify the functional diversity of AMPA-Rs. The significance and magnitude of molecular diversity, however, remain elusive. To gain insight into the molecular complexity of AMPA and kainate receptors, we compared the proteins that copurify with each receptor type in the rat brain...
June 28, 2012: Cell Reports
https://www.readbyqxmd.com/read/22120523/unexpected-diversity-in-shisa-like-proteins-suggests-the-importance-of-their-roles-as-transmembrane-adaptors
#10
Jimin Pei, Nick V Grishin
The Shisa family of single-transmembrane proteins is characterized by an N-terminal cysteine-rich domain and a proline-rich C-terminal region. Its founding member, Xenopus Shisa, promotes head development by antagonizing Wnt and FGF signaling. Recently, a mouse brain-specific Shisa protein CKAMP44 (Shisa9) was shown to play an important role in AMPA receptor desensitization. We used sequence similarity searches against protein, genome and EST databases to study the evolutionary origin and phylogenetic distribution of Shisa homologs...
March 2012: Cellular Signalling
https://www.readbyqxmd.com/read/20185686/ckamp44-a-brain-specific-protein-attenuating-short-term-synaptic-plasticity-in-the-dentate-gyrus
#11
Jakob von Engelhardt, Volker Mack, Rolf Sprengel, Netta Kavenstock, Ka Wan Li, Yael Stern-Bach, August B Smit, Peter H Seeburg, Hannah Monyer
CKAMP44, identified here by a proteomic approach, is a brain-specific type I transmembrane protein that associates with AMPA receptors in synaptic spines. CKAMP44 expressed in Xenopus oocytes reduced GluA1- and A2-mediated steady-state currents, but did not affect kainate- or N-methyl-D-aspartate (NMDA) receptor-mediated currents. Mouse hippocampal CA1 pyramidal neurons expressed CKAMP44 at low abundance, and overexpression of CKAMP44 led to stronger and faster AMPA receptor desensitization, slower recovery from desensitization, and a reduction in the paired-pulse ratio of AMPA currents...
March 19, 2010: Science
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