Sarcolipin alters SERCA1a interdomain communication by impairing binding of both calcium and ATP - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Scientific Reports Année : 2021

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

Résumé

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.
Fichier principal
Vignette du fichier
Mont1.pdf (1.58 Mo) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-03129096 , version 1 (19-05-2021)

Licence

Paternité

Identifiants

Citer

Cédric Montigny, Dong Liang Huang, Veronica Beswick, Thomas Barbot, Christine Jaxel, et al.. Sarcolipin alters SERCA1a interdomain communication by impairing binding of both calcium and ATP. Scientific Reports, 2021, 11 (1), pp.1641. ⟨10.1038/s41598-021-81061-6⟩. ⟨hal-03129096⟩
64 Consultations
22 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More