TY - JOUR
T1 - The golgin family exhibits a propensity to form condensates in living cells
AU - Ziltener, Pascal
AU - Rebane, Aleksander A.
AU - Graham, Morven
AU - Ernst, Andreas M.
AU - Rothman, James E.
N1 - Funding Information:
This work was supported by a NIH MIRA grant to J.E.R. (GM118084). We thank Al Mennone at the Yale Center for Cellular and Molecular Imaging Facility (CCMI, NIH grant S10OD020142) and Gouzel Tokmoulina at the Yale Flow Cytometry facility for assistance with cell sorting. We thank Xiaolei Su for valuable discussions.
Funding Information:
This work was supported by a NIH MIRA grant to J.E.R. (GM118084). We thank Al Mennone at the Yale Center for Cellular and Molecular Imaging Facility (CCMI, NIH grant S10OD020142) and Gouzel Tokmoulina at the Yale Flow Cytometry facility for assistance with cell sorting. We thank Xiaolei Su for valuable discussions.
Publisher Copyright:
© 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies
PY - 2020/10/1
Y1 - 2020/10/1
N2 - The Golgi is surrounded by a ribosome-excluding matrix. Recently, we reported that the cis-Golgi-localized golgin GM130 can phase-separate to form dynamic, liquid-like condensates in vitro and in vivo. Here, we show that the overexpression of each of the remaining cis (golgin160, GMAP210)- and trans (golgin97, golgin245, GCC88, GCC185)-golgins results in novel protein condensates. Focused ion beam scanning electron microscopy (FIB-SEM) images of GM130 condensates reveal a complex internal organization with branching aqueous channels. Pairs of golgins overexpressed in the same cell form distinct juxtaposed condensates. These findings support the hypothesis that, in addition to their established roles as vesicle tethers, phase separation may be a common feature of the golgin family that contributes to Golgi organization.
AB - The Golgi is surrounded by a ribosome-excluding matrix. Recently, we reported that the cis-Golgi-localized golgin GM130 can phase-separate to form dynamic, liquid-like condensates in vitro and in vivo. Here, we show that the overexpression of each of the remaining cis (golgin160, GMAP210)- and trans (golgin97, golgin245, GCC88, GCC185)-golgins results in novel protein condensates. Focused ion beam scanning electron microscopy (FIB-SEM) images of GM130 condensates reveal a complex internal organization with branching aqueous channels. Pairs of golgins overexpressed in the same cell form distinct juxtaposed condensates. These findings support the hypothesis that, in addition to their established roles as vesicle tethers, phase separation may be a common feature of the golgin family that contributes to Golgi organization.
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U2 - 10.1002/1873-3468.13884
DO - 10.1002/1873-3468.13884
M3 - Article
C2 - 32668013
AN - SCOPUS:85088783225
SN - 0014-5793
VL - 594
SP - 3086
EP - 3094
JO - FEBS Letters
JF - FEBS Letters
IS - 19
ER -