Sarcolipin alters SERCA1a interdomain communication by impairing binding of both calcium and ATP
| Autor: | Montigny, Cédric, Huang, Dong Liang, Beswick, Veronica, Barbot, Thomas, Jaxel, Christine, le Maire, Marc, Zheng, Ji-Shen, Jamin, Nadège |
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| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Protéines et Systèmes Membranaires (LPSM), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), University of Science and Technology of China [Hefei] (USTC), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proteolipids
Science [SDV]Life Sciences [q-bio] Muscle Proteins Saccharomyces cerevisiae Biochemistry Article Recombinant Proteins Sarcoplasmic Reticulum Calcium-Transporting ATPases Kinetics Adenosine Triphosphate Allosteric Regulation Enzyme mechanisms Membrane proteins Animals Medicine Calcium Rabbits Phosphorylation Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Nature Publishing Group, 2021, 11 (1), pp.1641. ⟨10.1038/s41598-021-81061-6⟩ Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021) Scientific Reports, 2021, 11 (1), pp.1641. ⟨10.1038/s41598-021-81061-6⟩ |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/s41598-021-81061-6⟩ |
| Popis: | Number: 1 Publisher: Nature Publishing Group; International audience; Sarcolipin (SLN), a single-spanning membrane protein, is a regulator of the sarco-endoplasmic reticulum Ca$^{2+}$-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$_2$.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. |
| Databáze: | OpenAIRE |
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