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1.2. Endoplasmic Reticulum (ER) stress: role of the B-cell lymphoma 2 (Bcl-2) Ca 2+ rheostat in cell death and survival. The ER plays a critical role in Ca 2+ handling, protein synthesis and protein processing [2-5].Impairment of these functions occurs in various pathological conditions resulting in the accumulation of misfolded proteins in the ER, which initiates the ER stress response [6-8].
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InoRos, Baciary · Song · 2012
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PLN inhibition of SERCA controls the rate of relaxation and the SR calcium load for subsequent contractions, modulating both the lusitropic and inotropic properties of the heart. PLN inhibition of SERCA is relieved by phosphorylation with the main mechanism involving protein kinase A (PKA) and the β-adrenergic pathway (Kirchberber et al., 1975).
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1. Introduction. Sarcoendoplasmic reticulum calcium ATPase (SERCA) is a transmembrane pump critical for Ca 2+ transport from the cytosol into the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscle cells, and into the endoplasmic reticulum (ER) of non-muscle cells [].The protein structure is highly conserved, exhibiting variations only in the extension of the C-terminal region.
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Sarco(endo)plasmic reticulum Ca 2+-ATPase (SERCA) is a membrane-bound transporter that pumps calcium ions from the cytosol into the lumen of the sarcoplasmic reticulum (SR) following muscle contraction.High SERCA activity is crucial for rapid contraction rates in muscles (Rome and Lindstedt, 1998), as the transporter restores both cytosolic and SR calcium levels that are necessary for.
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The systems of Ca 2+ homeostasis in nerve cells mainly involve Ca 2+ buffer proteins that serve as sensors, and a variety of Ca 2+-binding transmembrane channels (Berridge et al. 1998, 2000; Brini et al. 2014; Grienberger and Konnerth 2012).Due to its critical role in serving as carrier of critical information, cells must maintain low intracellular Ca 2+ levels, so that its concentration can.
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Schematic diagram of the structure of sarcoendoplasmic reticulum calcium ATPase (SERCA). The 3-dimensional crystal structure shows a SERCA pump in the ADP- and Ca 2+-bound state.D351 (in red) is the residue phosphorylated during the movement of Ca 2+ ions into the ER or SR. The three cytoplasmic domains, phosphorylation (P), nucleotide binding (N), and actuator (A) are labeled.