Loss of Extended Synaptotagmins ESyt2 and ESyt3 does not affect mouse development or viability, but in vitro cell migration and survival under stress are affected

@article{Herdman2014LossOE,
  title={Loss of Extended Synaptotagmins ESyt2 and ESyt3 does not affect mouse development or viability, but in vitro cell migration and survival under stress are affected},
  author={Chelsea Herdman and Michel G. Tremblay and P. K. Mishra and T. Moss},
  journal={Cell Cycle},
  year={2014},
  volume={13},
  pages={2616 - 2625}
}
The Extended Synaptotagmins (Esyts) are a family of multi-C2 domain membrane proteins with orthologs in organisms from yeast to human. Three Esyt genes exist in mouse and human and these have most recently been implicated in the formation of junctions between endoplasmic reticulum and plasma membrane, as well as the Ca2+ dependent replenishment of membrane phospholipids. The data are consistent with a function in extracellular signal transduction and cell adhesion, and indeed Esyt2 was… Expand
Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum Dysfunction
TLDR
In mice ESyts do not perform an essential role in basic cellular functions, suggesting that these highly conserved proteins may perform a specialized role that may manifest only during specific, as yet untested challenges. Expand
Loss of all 3 Extended Synaptotagmins does not affect normal mouse development, viability or fertility
TLDR
It is shown that E-Syt1 is specifically expressed throughout the embryonic skeleton during the early stages of chrondrogenesis in a pattern quite distinct from that of E- Syt2 or 3, suggesting that they may only provide a survival advantage under specific conditions that have as yet to be identified. Expand
Extended synaptotagmin interaction with the fibroblast growth factor receptor depends on receptor conformation, not catalytic activity.
TLDR
It is shown that ESyt2 is directed to the ER by its putative transmembrane domain, that the ESyts hetero- and homodimerize, and thatESyt2homodimerization in vivo requires a TM adjacent sequence but not the SMP domain. Expand
Extended synaptotagmin regulates plasma membrane-endoplasmic reticulum contact site structure and lipid transfer function in vivo
TLDR
It is reported that in Drosophila photoreceptors, MCS number is regulated by PLCβ activity and dEsyt function and PLC β signaling regulate ER-PM MCS structure and lipid transfer in DosophilaPhotoreceptor. Expand
The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses1[OPEN]
TLDR
Biochemical and physiological analyses indicate that SYT1 might function as an electrostatic phospholipid anchor conferring mechanical stability in plant cells, highlighting a putative role of plant ER-PM contact site components in the cellular adaptation to environmental stresses. Expand
Extended Synaptotagmin Interaction with the Fibroblast Growth Factor Receptor Depends on Receptor Conformation, Not Catalytic Activity*
TLDR
ESyt2 is directed to the ER by its putative transmembrane domain, that the ESyts hetero- and homodimerize, and that ESyt2Homodimerization in vivo requires a TM adjacent sequence but not the SMP domain. Expand
Extended synaptotagmin regulates membrane contact site structure and lipid transfer function in vivo
TLDR
It is reported that in Drosophila photoreceptors, MCS number is regulated by PLCβ activity and dEsyt function and PLC β signaling regulate ER‐PM MCS structure and lipid transfer in DosophilaPhotoreceptor. Expand
Lipid transporter TMEM24/C2CD2L is a Ca2+-regulated component of ER–plasma membrane contacts in mammalian neurons
TLDR
The present study identifies the phospholipid transporter TMEM24/C2CD2L as a regulated component of ER–PM contacts in neurons and suggests that lipid transfer between the two bilayers participates in the control of neuronal signaling. Expand
Unveiling physiological functions of extended synaptotagmins
TLDR
Findings suggest that the E-Syts not only mediate membrane tethering at ER-PM junctions but also contribute to cell signaling. Expand
The Step-Wise C-Truncation and Transport of ESyt3 to Lipid Droplets Reveals a Mother Primordial Cisterna
TLDR
Electron tomography-based 3D reconstruction of the fragmented primordial cisterna revealed patches of a tightly packed E-Syt3-rich network of varicose tubules in close contact with young LDs, which effectively inhibits LD biogenesis and growth. Expand
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