Extended synaptotagmin regulates membrane contact site structure and lipid transfer function in vivo
| Autor: | Shirish Mishra, Vaisaly R Nath, Bishal Basak, Deepti Trivedi, Padinjat Raghu |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Retinal degeneration
Mutant Endoplasmic Reticulum Biochemistry Synaptotagmin 1 Synaptotagmins 03 medical and health sciences 0302 clinical medicine Genetics medicine Animals Molecular Biology 030304 developmental biology 0303 health sciences Chemistry Cell Membrane Articles medicine.disease Lipids Null allele Membrane contact site humanities Cell biology Plant lipid transfer proteins 030217 neurology & neurosurgery Function (biology) Signal Transduction |
| Zdroj: | EMBO Rep |
| ISSN: | 1469-3178 1469-221X |
| DOI: | 10.15252/embr.202050264 |
| Popis: | Inter‐organelle communication between closely apposed membranes is proposed at membrane contact sites (MCS). However, the regulation of MCS structure and their functional relevance in vivo remain debated. The extended synaptotagmins (Esyt) are evolutionarily conserved proteins proposed to function at MCS. However, loss of all three Esyts in yeast or mammals shows minimal phenotypes questioning the functional importance of Esyt. We report that in Drosophila photoreceptors, MCS number is regulated by PLCβ activity. Photoreceptors of a null allele of Drosophila extended synaptotagmin (dEsyt) show loss of ER‐PM MCS. Loss of dEsyt results in mislocalization of RDGB, an MCS localized lipid transfer protein, required for photoreceptor structure and function, ultimately leading to retinal degeneration. dEsyt depletion enhanced the retinal degeneration, reduced light responses and slower rates of plasma membrane PIP (2) resynthesis seen in rdgB mutants. Thus, dEsyt function and PLCβ signaling regulate ER‐PM MCS structure and lipid transfer in Drosophila photoreceptors. |
| Databáze: | OpenAIRE |
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