The structure and flexibility analysis of the Arabidopsis Synaptotagmin 1 reveal the basis of its regulation at membrane contact sites
| Autor: | Noemi Ruiz-Lopez, María José Sánchez-Barrena, Dritan Siliqi, Armando Albert, Alberto Mills, Laura Lagartera, Federico Gago, Juan Luis Benavente, Lourdes Infantes, Miguel A. Botella |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España), ALBA Synchrotron |
| Rok vydání: | 2021 |
| Předmět: |
Health
Toxicology and Mutagenesis Protein Data Bank (RCSB PDB) SYT1 Biochemistry Genetics and Molecular Biology (miscellaneous) Synaptotagmin 1 Synaptotagmins chemistry.chemical_compound Arabidopsis Organelle structural biology Phosphatidylinositol C2 domain Ecology biology Chemistry Endoplasmic reticulum SAXS computer.file_format biology.organism_classification Protein Data Bank A-site plant science Biophysics lipids (amino acids peptides and proteins) computer Plant lipid transfer proteins |
| Zdroj: | EMBO journal (Online) 4 (2021). doi:10.26508/LSA.202101152 info:cnr-pdr/source/autori:Benavente J.L.; Siliqi D.; Infantes L.; Lagartera L.; Mills A.; Gago F.; Ruiz-Lopez N.; Botella M.A.; Sanchez-Barrena M.J.; Albert A./titolo:The structure and flexibility analysis of the Arabidopsis synaptotagmin 1 reveal the basis of its regulation at membrane contact sites/doi:10.26508%2FLSA.202101152/rivista:EMBO journal (Online)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:4 Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | 17 pags., 7 figs., 1 tab. Non-vesicular lipid transfer at ER and plasma membrane (PM) contact sites (CS) is crucial for the maintenance of membrane lipid homeostasis. Extended synaptotagmins (E-Syts) play a central role in this process as they act as molecular tethers of ER and PM and as lipid transfer proteins between these organelles. E-Syts are proteins constitutively anchored to the ER through an N-terminal hydrophobic segment and bind the PM via a variable number of C-terminal C2 domains. Synaptotagmins (SYTs) are the plant orthologous of E-Syts and regulate the ER–PM communication in response to abiotic stress. Combining different structural and biochemical techniques, we demonstrate that the binding of SYT1 to lipids occurs through a Ca2+-dependent lipid-binding site and by a site for phosphorylated forms of phosphatidylinositol, thus integrating two different molecular signals in response to stress. In addition, we show that SYT1 displays three highly flexible hinge points that provide conformational freedom to facilitate lipid extraction, protein loading, and subsequent transfer between PM and ER. This work was funded by grants from Agencia Estatal de Investigación (AEI, Spain) and Fondo Europeo de Desarrollo Regional (European Union) (BIO2017-89523-R to A Albert). A Albert and D Siliqi thank ALBA (beamline XALOC) and Diamond Light Source (beamline B21, proposal MX21741) for granting access to the synchrotron radiation source. We thank Nathan Cowieson and Charlotte JC Edwards-Gayle from Diamond Light Source for their assistance in the preparation of the SAXS experiments |
| Databáze: | OpenAIRE |
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