scholarly journals Structure and function of ER membrane contact sites with other organelles

2015 ◽  
Vol 17 (2) ◽  
pp. 69-82 ◽  
Author(s):  
Melissa J. Phillips ◽  
Gia K. Voeltz
Keyword(s):  
Structure And Function ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
And Function ◽  
Er Membrane

scholarly journals Calcium signaling at ER membrane contact sites

2015 ◽  
Vol 1853 (9) ◽  
pp. 2012-2017 ◽  
Author(s):  
Thomas Burgoyne ◽  
Sandip Patel ◽  
Emily R. Eden
Keyword(s):  
Calcium Signaling ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
Er Membrane

scholarly journals Organization and function of membrane contact sites

2013 ◽  
Vol 1833 (11) ◽  
pp. 2526-2541 ◽  
Author(s):  
Sebastian C.J. Helle ◽  
Gil Kanfer ◽  
Katja Kolar ◽  
Alexander Lang ◽  
Agnès H. Michel ◽  
...  
Keyword(s):  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
And Function

scholarly journals Stitching Organelles: Organization and Function of Specialized Membrane Contact Sites in Plants

2016 ◽  
Vol 26 (9) ◽  
pp. 705-717 ◽  
Author(s):  
Jessica Pérez-Sancho ◽  
Jens Tilsner ◽  
A. Lacey Samuels ◽  
Miguel A. Botella ◽  
Emmanuelle M. Bayer ◽  
...  
Keyword(s):  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
And Function

scholarly journals Endoplasmic Reticulum‐Plasma Membrane Contact Sites as an Organizing Principle for Compartmentalized Calcium and cAMP Signaling

2021 ◽  
Vol 22 (9) ◽  
pp. 4703
Author(s):  
Tim Crul ◽  
József Maléth
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Second Messengers ◽  
Adenosine Monophosphate ◽  
Camp Signaling ◽  
Cell Physiology ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact ◽  
Er Membrane

In eukaryotic cells, ultimate specificity in activation and action—for example, by means of second messengers—of the myriad of signaling cascades is primordial. In fact, versatile and ubiquitous second messengers, such as calcium (Ca2+) and cyclic adenosine monophosphate (cAMP), regulate multiple—sometimes opposite—cellular functions in a specific spatiotemporal manner. Cells achieve this through segregation of the initiators and modulators to specific plasma membrane (PM) subdomains, such as lipid rafts and caveolae, as well as by dynamic close contacts between the endoplasmic reticulum (ER) membrane and other intracellular organelles, including the PM. Especially, these membrane contact sites (MCSs) are currently receiving a lot of attention as their large influence on cell signaling regulation and cell physiology is increasingly appreciated. Depletion of ER Ca2+ stores activates ER membrane STIM proteins, which activate PM-residing Orai and TRPC Ca2+ channels at ER–PM contact sites. Within the MCS, Ca2+ fluxes relay to cAMP signaling through highly interconnected networks. However, the precise mechanisms of MCS formation and the influence of their dynamic lipid environment on their functional maintenance are not completely understood. The current review aims to provide an overview of our current understanding and to identify open questions of the field.

scholarly journals SAC1 Degrades its Lipid Substrate PtdIns4P in the Endoplasmic Reticulum to Maintain a Steep Chemical Gradient with Donor Membranes

2018 ◽  
Author(s):  
James P. Zewe ◽  
Rachel C. Wills ◽  
Sahana Sangappa ◽  
Brady D. Goulden ◽  
Gerald R. V. Hammond
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Homeostasis ◽  
Chemical Gradient ◽  
Vesicular Traffic ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Catalytic Domains ◽  
In Trans ◽  
Membrane Contact ◽  
And Function

AbstractGradients of PtdIns4P between organelle membranes and the endoplasmic reticulum (ER) are thought to drive counter-transport of other lipids via non-vesicular traffic. This novel pathway requires the SAC1 phosphatase to degrade PtdIns4P in a “cis” configuration at the ER to maintain the gradient. However, SAC1 has also been proposed to act in “trans” at membrane contact sites, which could oppose lipid traffic. It is therefore crucial to determine which mode SAC1 uses in living cells. We report that acute inhibition of SAC1 causes accumulation of PtdIns4P in the ER, that SAC1 does not enrich at membrane contact sites, and that SAC1 has little activity in “trans”, unless a linker is added between its ER-anchored and catalytic domains. The data reveal an obligate “cis” activity of SAC1, supporting its role in non-vesicular lipid traffic and implicating lipid traffic more broadly in inositol lipid homeostasis and function.

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