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肌联蛋白通过破坏钙和 ATP 的结合来改变 SERCA1a 结构域间的通讯。

Sarcolipin alters SERCA1a interdomain communication by impairing binding of both calcium and ATP.

机构信息

CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, 91198, Gif-sur-Yvette, France.

Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, 230027, China.

出版信息

Sci Rep. 2021 Jan 15;11(1):1641. doi: 10.1038/s41598-021-81061-6.

DOI:10.1038/s41598-021-81061-6
PMID:33452371
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7810697/
Abstract

Sarcolipin (SLN), a single-spanning membrane protein, is a regulator of the sarco-endoplasmic reticulum Ca-ATPase (SERCA1a). Chemically synthesized SLN, palmitoylated or not (pSLN or SLN), and recombinant wild-type rabbit SERCA1a expressed in S. cerevisiae design experimental conditions that provide a deeper understanding of the functional role of SLN on the regulation of SERCA1a. Our data show that chemically synthesized SLN interacts with recombinant SERCA1a, with calcium-deprived E2 state as well as with calcium-bound E1 state. This interaction hampers the binding of calcium in agreement with published data. Unexpectedly, SLN has also an allosteric effect on SERCA1a transport activity by impairing the binding of ATP. Our results reveal that SLN significantly slows down the E2 to Ca.E1 transition of SERCA1a while it affects neither phosphorylation nor dephosphorylation. Comparison with chemically synthesized SLN deprived of acylation demonstrates that palmitoylation is not necessary for either inhibition or association with SERCA1a. However, it has a small but statistically significant effect on SERCA1a phosphorylation when various ratios of SLN-SERCA1a or pSLN-SERCA1a are tested.

摘要

肌联蛋白（SLN）是一种单跨膜蛋白，是肌浆内质网 Ca-ATP 酶（SERCA1a）的调节剂。化学合成的 SLN，棕榈酰化或非棕榈酰化（pSLN 或 SLN），以及在酿酒酵母中表达的重组野生型兔 SERCA1a，设计的实验条件提供了对 SLN 对 SERCA1a 调节的功能作用的更深入理解。我们的数据表明，化学合成的 SLN 与重组 SERCA1a 相互作用，与钙剥夺的 E2 状态以及与钙结合的 E1 状态相互作用。这种相互作用与已发表的数据一致，阻碍了钙的结合。出乎意料的是，SLN 对 SERCA1a 转运活性也具有变构效应，通过损害 ATP 的结合。我们的结果表明，SLN 显著减慢了 SERCA1a 的 E2 到 Ca.E1 转变，而对磷酸化或去磷酸化没有影响。与缺乏酰化的化学合成 SLN 的比较表明，棕榈酰化对于与 SERCA1a 的抑制或结合都不是必需的。然而，当测试各种 SLN-SERCA1a 或 pSLN-SERCA1a 的比例时，它对 SERCA1a 的磷酸化有一个小但具有统计学意义的影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/df3e38a95676/41598_2021_81061_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/98f288bfaf79/41598_2021_81061_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/c5fd2f3f16d8/41598_2021_81061_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/9e75f6542612/41598_2021_81061_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/f58d50ff63d3/41598_2021_81061_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/a0a693ae4fdf/41598_2021_81061_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/df3e38a95676/41598_2021_81061_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/98f288bfaf79/41598_2021_81061_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/c5fd2f3f16d8/41598_2021_81061_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/9e75f6542612/41598_2021_81061_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/f58d50ff63d3/41598_2021_81061_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/a0a693ae4fdf/41598_2021_81061_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a511/7810697/df3e38a95676/41598_2021_81061_Fig6_HTML.jpg

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The SERCA residue Glu340 mediates interdomain communication that guides Ca transport.SERCA 残基 Glu340 介导结构域间通讯，指导 Ca 转运。
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