2-Aminoethoxydiphenyl borate directly facilitates and indirectly inhibits STIM1-dependent gating of CRAC channels
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چکیده
منابع مشابه
2-aminoethoxydiphenyl borate directly inhibits channels composed of connexin26 and/or connexin32.
2-aminoethoxydiphenyl borate (2-APB), a commonly used blocker of IP3-induced calcium ion release and of store-operated channels, inhibits gap junction conductance when applied to cultured cells. The character and pharmacology of this inhibition was explored using 1) hemichannels composed of connexin32 (Cx32) and/or connexin26 (Cx26) purified from native sources and from transfected HeLa cells i...
متن کامل2-Aminoethoxydiphenyl Borate Potentiates CRAC Current by Directly Dilating the Pore of Open Orai1
2-Aminoethoxydiphenyl borate (2-APB) elicits potentiation current (Ip) on Ca(2+) release-activated Ca(2+) (CRAC) channels. An accurate investigation into this modulation mechanism would reveal how STIM1-dependent channel gating is enhanced, and benefit the future immune enhancer development. Here, we directly probed the pore diameter of CRAC channels and found that 2-APB enlarged the pore size ...
متن کامل2-Aminoethoxydiphenyl borate directly inhibits store-operated calcium entry channels in human platelets.
In this study, we examined 2-aminoethoxydiphenyl borate (2APB) as an inhibitor of Ca(2+) influx in human platelets. 2APB was found to inhibit thrombin-mediated intracellular Ca(2+) mobilization rapidly in platelets incubated in the absence of extracellular Ca(2+). This result supports an intracellular action of 2APB on inositol 1,4,5-trisphosphate (IP(3))-receptor Ca(2+) channels. 2APB was with...
متن کاملA single lysine in the N-terminal region of store-operated channels is critical for STIM1-mediated gating
Store-operated Ca(2+) entry is controlled by the interaction of stromal interaction molecules (STIMs) acting as endoplasmic reticulum ER Ca(2+) sensors with calcium release-activated calcium (CRAC) channels (CRACM1/2/3 or Orai1/2/3) in the plasma membrane. Here, we report structural requirements of STIM1-mediated activation of CRACM1 and CRACM3 using truncations, point mutations, and CRACM1/CRA...
متن کاملSTIM1 and calmodulin interact with Orai1 to induce Ca2+-dependent inactivation of CRAC channels.
Ca(2+)-dependent inactivation (CDI) is a key regulator and hallmark of the Ca(2+) release-activated Ca(2+) (CRAC) channel, a prototypic store-operated Ca(2+) channel. Although the roles of the endoplasmic reticulum Ca(2+) sensor STIM1 and the channel subunit Orai1 in CRAC channel activation are becoming well understood, the molecular basis of CDI remains unclear. Recently, we defined a minimal ...
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ژورنال
عنوان ژورنال: The Journal of Physiology
سال: 2008
ISSN: 0022-3751
DOI: 10.1113/jphysiol.2008.151365