TY - JOUR
T1 - Lam6 Regulates the Extent of Contacts between Organelles
AU - Elbaz-Alon, Yael
AU - Eisenberg-Bord, Michal
AU - Shinder, Vera
AU - Stiller, Sebastian Berthold
AU - Shimoni, Eyal
AU - Wiedemann, Nils
AU - Geiger, Tamar
AU - Schuldiner, Maya
N1 - Publisher Copyright:
© 2015 The Authors.
PY - 2015/7/7
Y1 - 2015/7/7
N2 - Communication between organelles is crucial for eukaryotic cells to function as one coherent unit. Animportant means of communication is through membrane contact sites, where two organelles come into close proximity allowing the transport of lipids and small solutes between them. Contact sites are dynamic in size and can change in response to environmental or cellular stimuli; however, how this is regulated has been unclear. Here, we show that Saccharomyces cerevisiae Lam6 resides in several central contact sites: ERMES (ER/mitochondria encounter structure), vCLAMP (vacuole and mitochondria patch), and NVJ (nuclear vacuolar junction). Weshow that Lam6 is sufficient for expansion of contact sites under physiological conditions and necessary for coordination of contact site size. Given that Lam6 is part of a large protein family and is conserved in vertebrates, our work opens avenues for investigating the underlying principles of organelle communication.
AB - Communication between organelles is crucial for eukaryotic cells to function as one coherent unit. Animportant means of communication is through membrane contact sites, where two organelles come into close proximity allowing the transport of lipids and small solutes between them. Contact sites are dynamic in size and can change in response to environmental or cellular stimuli; however, how this is regulated has been unclear. Here, we show that Saccharomyces cerevisiae Lam6 resides in several central contact sites: ERMES (ER/mitochondria encounter structure), vCLAMP (vacuole and mitochondria patch), and NVJ (nuclear vacuolar junction). Weshow that Lam6 is sufficient for expansion of contact sites under physiological conditions and necessary for coordination of contact site size. Given that Lam6 is part of a large protein family and is conserved in vertebrates, our work opens avenues for investigating the underlying principles of organelle communication.
UR - http://www.scopus.com/inward/record.url?scp=84937515326&partnerID=8YFLogxK
U2 - 10.1016/j.celrep.2015.06.022
DO - 10.1016/j.celrep.2015.06.022
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C2 - 26119743
AN - SCOPUS:84937515326
SN - 2211-1247
VL - 12
SP - 7
EP - 14
JO - Cell Reports
JF - Cell Reports
IS - 1
ER -