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On the function of pentameric phospholamban: ion channel or storage form?五聚体受磷蛋白的功能：离子通道还是储存形式？
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2
The Phospholamban Pentamer Alters Function of the Sarcoplasmic Reticulum Calcium Pump SERCA.磷酸化肌浆网钙转运蛋白五聚体改变肌浆网钙泵 SERCA 的功能。
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3
Phospholamban spontaneously reconstitutes into giant unilamellar vesicles where it generates a cation selective channel.受磷蛋白可自发重组形成巨型单层囊泡，在其中形成阳离子选择性通道。
Phys Chem Chem Phys. 2016 Jan 21;18(3):1629-36. doi: 10.1039/c5cp05893g. Epub 2015 Dec 17.
4
Phospholamban phosphorylation increases the passive calcium leak from cardiac sarcoplasmic reticulum.肌浆网磷蛋白磷酸化增加了心肌肌浆网的被动钙离子漏。
Pflugers Arch. 2012 Sep;464(3):295-305. doi: 10.1007/s00424-012-1124-9. Epub 2012 Jul 7.
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The structure of phospholamban pentamer reveals a channel-like architecture in membranes.受磷蛋白五聚体的结构揭示了膜中类似通道的结构。
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Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.通过混合溶液和固态 NMR 方法研究磷脂酶抑制剂五聚体在双层脂膜中的结构拓扑。
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HNO enhances SERCA2a activity and cardiomyocyte function by promoting redox-dependent phospholamban oligomerization.HNO 通过促进氧化还原依赖的肌球蛋白轻链磷酸酶锚定蛋白寡聚化来增强 SERCA2a 活性和心肌细胞功能。
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Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport.磷酸化肌浆球蛋白结合蛋白同五聚体的结构动力学和拓扑结构揭示了其在钙转运调节中的作用。
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Regulation of the calcium ion pump of sarcoplasmic reticulum: reversible inhibition by phospholamban and by the calmodulin binding domain of the plasma membrane calcium ion pump.肌浆网钙离子泵的调节：受受磷蛋白以及质膜钙离子泵的钙调蛋白结合域的可逆抑制。
Biochemistry. 1992 Jan 21;31(2):371-6. doi: 10.1021/bi00117a009.

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Carbonic anhydrase 2-derived drug-responsive domain regulates membrane-bound cytokine expression and function in engineered T cells.碳酸酐酶2衍生的药物反应域调节工程T细胞中膜结合细胞因子的表达和功能。
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General rules for the arrangements and gating motions of pore-lining helices in homomeric ion channels.同聚体离子通道中孔道内衬螺旋的排列和门控运动的一般规则。
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Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.通过固态核磁共振受限模拟研究膜中SERCA调节蛋白的结构动力学和构象平衡。
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Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport.磷酸化肌浆球蛋白结合蛋白同五聚体的结构动力学和拓扑结构揭示了其在钙转运调节中的作用。
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10
Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.肌浆球蛋白结合蛋白 C 的激发态结构及其磷酸化时的构象变化。
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本文引用的文献

1
Molecular dynamics studies on structure and dynamics of phospholamban monomer and pentamer in membranes.膜中受磷蛋白单体和五聚体的结构与动力学的分子动力学研究。
Proteins. 2009 Jul;76(1):86-98. doi: 10.1002/prot.22322.
2
Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex.模拟磷酸化突变增加了受磷蛋白的寡聚化并改变了其调节复合物的结构。
J Biol Chem. 2008 Oct 24;283(43):28996-9003. doi: 10.1074/jbc.M804782200. Epub 2008 Aug 16.
3
Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells.通过荧光共振能量转移在活细胞中测量受磷蛋白寡聚化、四级结构和肌浆（内质）网钙ATP酶结合情况。
J Biol Chem. 2008 May 2;283(18):12202-11. doi: 10.1074/jbc.M707590200. Epub 2008 Feb 19.
4
Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.受磷蛋白和肌浆脂质蛋白抑制的Ca(2+) -ATP酶的结构与动力学基础
Biochemistry. 2008 Jan 8;47(1):3-13. doi: 10.1021/bi701668v. Epub 2007 Dec 15.
5
Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.膜双层中磷酸受纳蛋白五聚体跨膜区和近膜区的结构限制：谷氨酰胺29和亮氨酸52
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Calcium cycling and signaling in cardiac myocytes.心肌细胞中的钙循环与信号传导。
Annu Rev Physiol. 2008;70:23-49. doi: 10.1146/annurev.physiol.70.113006.100455.
7
Förster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex.荧光共振能量转移恢复实验表明，受磷蛋白从五聚体中交换缓慢，但从肌浆网钙ATP酶调节复合物中交换迅速。
Circ Res. 2007 Nov 26;101(11):1123-9. doi: 10.1161/CIRCRESAHA.107.159947. Epub 2007 Nov 1.
8
Spectroscopic validation of the pentameric structure of phospholamban.受磷蛋白五聚体结构的光谱验证
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9
Anatomy and dynamics of a supramolecular membrane protein cluster.超分子膜蛋白簇的结构与动力学
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10
An electrochemical investigation of sarcolipin reconstituted into a mercury-supported lipid bilayer.对重构于汞支撑脂质双分子层中的肌浆球蛋白的电化学研究。
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五聚体受磷蛋白的功能：离子通道还是储存形式？

On the function of pentameric phospholamban: ion channel or storage form?

作者信息

Becucci Lucia, Cembran Alessandro, Karim Christine B, Thomas David D, Guidelli Rolando, Gao Jiali, Veglia Gianluigi

出版信息

Biophys J. 2009 May 20;96(10):L60-2. doi: 10.1016/j.bpj.2009.03.013.

DOI:10.1016/j.bpj.2009.03.013
PMID:19450461
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2712152/
Abstract

Phospholamban (PLN) is an integral membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase, thereby regulating muscle contractility. We report a combined electrochemical and theoretical study demonstrating that the pentameric PLN does not possess channel activity for conducting chloride or calcium ions across the lipid membrane. This suggests that the pentameric configuration of PLN primarily serves as a storage form for the regulatory function of muscle relaxation by the PLN monomer.

摘要

受磷蛋白（PLN）是一种整合膜蛋白，可抑制肌浆网Ca(2+)-ATP酶，从而调节肌肉收缩力。我们报告了一项电化学与理论相结合的研究，结果表明五聚体PLN不具备使氯离子或钙离子穿过脂质膜的通道活性。这表明PLN的五聚体结构主要作为一种储存形式，用于发挥PLN单体对肌肉舒张的调节功能。