TY - JOUR
T1 - Molecular mechanisms of inter-organelle ER-PM contact sites
AU - Henne, W. Mike
AU - Liou, Jen
AU - Emr, Scott D.
N1 - Funding Information:
The authors would like to thank Chris Stefan and Joel Goodman for their helpful discussions in preparation of the manuscript. W.M.H. is a WW Caruth, Jr Scholar in Medical Research. J.L. is a Sowell Family Scholar in Medical Research. J.L. is supported by a Welch Foundation grant I-1789 . S.D.E. is supported by a Cornell University research grant. WM Henne is also supported by the Welch Foundation, under Grant I-1873.
Publisher Copyright:
© 2015 Elsevier Ltd.
PY - 2015/8/1
Y1 - 2015/8/1
N2 - Observed for decades by electron microscopy but mostly ignored, inter-organelle membrane contact sites (MCSs) are now emerging as major sites for the exchange of cellular components in eukaryotic cells. Although new MCSs are continually characterized, those formed between the endoplasmic reticulum (ER) and the plasma membrane (PM) are currently the best defined. Here, we focus on ER-PM contact sites as a model system for understanding the molecular mechanisms that govern inter-organelle junctions. Through tight inter-organelle tethering, ER-PM proteins generate a unique microenvironment optimized for processes like lipid and ion transport. Several MCS proteins also boast potential membrane remodeling domains, which may promote curvature and lipid transfer between juxtaposed bilayers. Finally, we discuss challenges and future directions for the MCS field.
AB - Observed for decades by electron microscopy but mostly ignored, inter-organelle membrane contact sites (MCSs) are now emerging as major sites for the exchange of cellular components in eukaryotic cells. Although new MCSs are continually characterized, those formed between the endoplasmic reticulum (ER) and the plasma membrane (PM) are currently the best defined. Here, we focus on ER-PM contact sites as a model system for understanding the molecular mechanisms that govern inter-organelle junctions. Through tight inter-organelle tethering, ER-PM proteins generate a unique microenvironment optimized for processes like lipid and ion transport. Several MCS proteins also boast potential membrane remodeling domains, which may promote curvature and lipid transfer between juxtaposed bilayers. Finally, we discuss challenges and future directions for the MCS field.
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U2 - 10.1016/j.ceb.2015.05.001
DO - 10.1016/j.ceb.2015.05.001
M3 - Review article
C2 - 26025028
AN - SCOPUS:84938696236
SN - 0955-0674
VL - 35
SP - 123
EP - 130
JO - Current Opinion in Cell Biology
JF - Current Opinion in Cell Biology
ER -