In VitroInteraction of Estradiol Receptor with Ca2+-Calmodulin
نویسندگان
چکیده
منابع مشابه
GTP binds to Rab3A in a complex with Ca2+/calmodulin.
Ras-like small GTP-binding proteins of the Rab family regulate trafficking of the secretory or endocytic pathways. Rab3 proteins within the Rab family are expressed at high levels in neurons and endocrine cells, where they regulate release of dense-core granules and synaptic vesicles (SVs). Rab3A is present as either the soluble or the SV membrane-bound form in neurons that are dependent on the...
متن کاملDifferential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration.
Multiple calmodulin (CaM) isoforms are expressed in plants, but their biochemical characteristics are not well resolved. Here we show the differential regulation exhibited by two soya bean CaM isoforms (SCaM-1 and SCaM-4) for the activation of five CaM-dependent enzymes, and the Ca(2+) dependence of their target enzyme activation. SCaM-1 activated myosin light-chain kinase as effectively as bra...
متن کاملConservation of Ca2+/Calmodulin Regulation across Na and Ca2+ Channels
Voltage-gated Na and Ca2+ channels comprise distinct ion channel superfamilies, yet the carboxy tails of these channels exhibit high homology, hinting at a long-shared and purposeful module. For different Ca2+ channels, carboxyl-tail interactions with calmodulin do elaborate robust and similar forms of Ca2+ regulation. However, Na channels have only shown subtler Ca2+ modulation that differs am...
متن کاملMechanism of Local and Global Ca2+ Sensing by Calmodulin in Complex with a Ca2+ Channel
Calmodulin (CaM) in complex with Ca(2+) channels constitutes a prototype for Ca(2+) sensors that are intimately colocalized with Ca(2+) sources. The C-lobe of CaM senses local, large Ca(2+) oscillations due to Ca(2+) influx from the host channel, and the N-lobe senses global, albeit diminutive Ca(2+) changes arising from distant sources. Though biologically essential, the mechanism underlying g...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Endocrinology
سال: 1988
ISSN: 0888-8809,1944-9917
DOI: 10.1210/mend-2-2-167