ASIC2 Subunits Target Acid-Sensing Ion Channels to the Synapse via an Association with PSD-95
Xiang-ming Zha,Margaret P. Price,Vivian Costa,Anne Marie S. Harding,Leah R. Reznikov,Chirstopher J Benson,Michael J. Welsh +6 more
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TLDR
Results indicate that ASIC2 facilitates ASIC1a localization and function in dendritic spines and suggest that the two subunits work in concert to regulate neuronal function.Abstract:
Acid-sensing ion channel-1a (ASIC1a) mediates H+-gated current to influence normal brain physiology and impact several models of disease. Although ASIC2 subunits are widely expressed in brain and modulate ASIC1a current, their function remains poorly understood. We identified ASIC2a in dendrites, dendritic spines, and brain synaptosomes. This localization largely relied on ASIC2a binding to PSD-95 and matched that of ASIC1a, which does not coimmunoprecipitate with PSD-95. We found that ASIC2 and ASIC1a associated in brain, and through its interaction with PSD-95, ASIC2 increased ASIC1a localization in dendritic spines. Consistent with earlier work showing that acidic pH elevated spine [Ca2+]i by activating ASIC1a, loss of ASIC2 decreased the percentage of spines responding to acid. Moreover, like a reduction of ASIC1a, the number of spine synapses fell in ASIC2−/− neurons. These results indicate that ASIC2 facilitates ASIC1a localization and function in dendritic spines and suggest that the two subunits work in concert to regulate neuronal function.read more
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疟原虫var基因转换速率变化导致抗原变异[英]/Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A
TL;DR: PfPMP1)与感染红细胞、树突状组胞以及胎盘的单个或多个受体作用,在黏附及免疫逃避中起关键的作�ly.
Journal ArticleDOI
Acid-Sensing Ion Channels in Glial Cells
Victoria Cegielski,Rohan Chakrabarty,Shinghua Ding,Michael J. Wacker,Paula Monaghan‐Nichols,Xiang-Ping Chu +5 more
TL;DR: Information on the unique ASIC components in each of the glial cells is concentrated on and integrates these glial-specific ASICs with their physiological and pathological conditions, providing promising evidence for targeting of ASICs in individualglial cells as a therapeutic strategy for a diverse range of conditions.
Journal ArticleDOI
Acid-Sensing Ion Channel 2: Function and Modulation
TL;DR: Evidence of the influence of ASIC2 influence in pathologies such as ischemic brain injury, multiple sclerosis, epilepsy, migraines, drug addiction, etc, substantiates the ASIC2 protein as a potential therapeutic target for various neurological, psychological, and cerebrovascular diseases.
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Neuronal potential of umbilical cord blood non-hematopoietic multipotent stem cells
TL;DR: In vitro modelling of human corticogenesis using umbilical cord blood stem cells, March 13-14, 2010, 3rd Pan Arab Human genetic conference, Dubai, United Arab Emirates.
References
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疟原虫var基因转换速率变化导致抗原变异[英]/Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A
TL;DR: PfPMP1)与感染红细胞、树突状组胞以及胎盘的单个或多个受体作用,在黏附及免疫逃避中起关键的作�ly.
Journal ArticleDOI
PDZ domain proteins of synapses
Eunjoon Kim,Morgan Sheng +1 more
TL;DR: PDZ domains are protein-interaction domains that are often found in multi-domain scaffolding proteins that function in the dynamic trafficking of synaptic proteins by assembling cargo complexes for transport by molecular motors.
Journal ArticleDOI
Driving AMPA Receptors into Synapses by LTP and CaMKII: Requirement for GluR1 and PDZ Domain Interaction
Yasunori Hayashi,Song-Hai Shi,José A. Esteban,Antonella Piccini,Jean Christophe Poncer,Roberto Malinow +5 more
TL;DR: Results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.
Journal ArticleDOI
Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
Zhou Songyang,Alan S. Fanning,C. Fu,Jian Xu,Shirin M. Marfatia,Athar H. Chishti,Anne M. Crompton,Andrew C. Chan,James M. Anderson,Lewis C. Cantley +9 more
TL;DR: On the basis of crystal structures of the PSD-95-3 PDZ domain, the specificities observed with the peptide library can be rationalized.
Journal ArticleDOI
A proton-gated cation channel involved in acid-sensing
TL;DR: The biophysical and pharmacological properties of the cloned H+-gated channel (ASIC), for acid-sensing ionic channel that belongs to the amilor-ide-sensitive Na+ channel6–1 Vdegenerin12–14 family of ion channels, closely match those described in sensory neurons.