Phospholamban domain i/cytochrome b5 transmembrane sequence chimeras do not inhibit serca2a
TL;DR: A series of chimeras between the transmembrane domains of phospholamban and cytochrome b 5 were coexpressed with the Ca2+‐ATPase of cardiac sarcoplasmic reticulum (SERCA2a) to show that cytoplasmic interactions regulate the inhibitory interactions in a four‐base circuit.
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About: This article is published in FEBS Letters. The article was published on 03 Apr 1998. and is currently open access. The article focuses on the topics: Transmembrane domain & Phospholamban.
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Citations
Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase.
TL;DR: This review focuses on the advances in the understanding of the regulation of SERCA2a by SLN and PLB and highlights the similarities and differences between the two proteins and their roles in cardiac patho-physiology.
147
Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone
TL;DR: The cytoplasmic domain of PLB is in a dynamic equilibrium between an ordered conformation which is in direct contact with the membrane surface, and a dynamically disordered form, which is detached from the membrane and poised to interact with its regulatory target.
134
Atomic-level mechanisms for phospholamban regulation of the calcium pump.
TL;DR: It is concluded that PLB-mediated regulation of SERCA activity in the heart results from biochemical and structural transitions that occur primarily in the E1 state of the pump.
40
Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases.
TL;DR: Results suggest that a SERCA1-PLN interaction site occurs between L67 ofSERCA1a and domain IB of PLN, which involves SERCA 1a D813 and PLN N27 and N30.
36
Patent
Signal for targeting molecules to the sarco(endo)plasmic reticulum
Thomas D. Reed
- 29 Nov 2003
TL;DR: In this paper, the authors proposed a method to target molecules to the sarco(endo)plasmic reticulum (SR) of eukaryotic cells by using polypeptide sequences as a localization signal.
14
References
Residues 2-25 of phospholamban are insufficient to inhibit Ca2+ transport ATPase of cardiac sarcoplasmic reticulum.
Larry R. Jones,Loren J. Field +1 more
TL;DR: It is concluded that the cytoplasmic domain of PLB, containing the phosphorylation sites, by itself is insufficient to inhibit the Ca2+ pump and that the transmembrane region, which stabilizes the pentamer, is also essential for Ca2- transport regulation.
52
An investigation of the mechanism of inhibition of the Ca2+-ATPase by phospholamban
TL;DR: Reconstitution with the hydrophobic domain of PLB was found to decrease the apparent affinity of the ATPase for Ca2+ with no effect on the maximal rate of ATP hydrolysis observed at saturating concentrations of Ca2+.
48
The hydrophilic domain of phospholamban inhibits the Ca2+ transport step of the Ca2+-ATPase
G Hughes,J M East,Anthony G. Lee +2 more
TL;DR: The peptide MEKVQYLTRSAIRRASTIEMPQQAR-Cys corresponding to residues 1-25 of phospholamban was found to inhibit the ATPase activity of skeletal muscle Ca(2+)-ATPase, but to have no effect on the Ca( 2+)-dependence of its activity.
47
Effects of monoclonal antibody against phospholamban on calcium pump ATPase of cardiac sarcoplasmic reticulum.
TL;DR: Results indicate that the binding of the antibody to phospholamban produces essentially the same mode of action on Ca2+ pump ATPase as that of phosphol amban phosphorylation, resulting in the stimulation of Ca2- pump.
41
Biochemical and biophysical comparison of native and chemically synthesized phospholamban and a monomeric phospholamban analog.
Ernest J. Mayer,Edward McKenna,Victor M. Garsky,Carl J. Burke,Henryk Mach,C. Russell Middaugh,Mohinder K. Sardana,Jeffrey S. Smith,Robert G. Johnson +8 more
TL;DR: Native and synthetic PLB reduced the calcium sensitivity of CaATPase, which is reversed by anti-PLB antibody, and the more readily available synthetic protein should be suitable for more extensive structural studies.
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