RT Journal Article
T1 Liquid–liquid phase separation of the Golgi matrix protein GM130
A1 Rebane, Aleksander A.
A1 Ziltener, Pascal
A1 LaMonica, Lauren C.
A1 Bauer, Antonia H.
A1 Zheng, Hong
A1 López-Montero, Iván
A1 Pincet, Frederic
A1 Rothman, James E.
A1 Ernst, Andreas M.
AB Golgins are an abundant class of peripheral membrane proteins of the Golgi. These very long (50–400 nm) rod-like proteins initially capture cognate transport vesicles, thus enabling subsequent SNARE-mediated membrane fusion. Here, we explore the hypothesis that in addition to serving as vesicle tethers, Golgins may also possess the capacity to phase separate and, thereby, contribute to the internal organization of the Golgi. GM130 is the most abundant Golgin at the cis Golgi. Remarkably, overexpressed GM130 forms liquid droplets in cells analogous to those described for numerous intrinsically disordered proteins with low complexity sequences, even though GM130 is neither low in complexity nor intrinsically disordered. Virtually pure recombinant GM130 also phase-separates into dynamic, liquid-like droplets in close to physiological buffers and at concentrations similar to its estimated local concentration at the cis Golgi.
PB John Wiley & Sons/Federation of European Biochemical Societies
SN 0014-5793
YR 2020
FD 2020
LK https://hdl.handle.net/20.500.14352/6183
UL https://hdl.handle.net/20.500.14352/6183
LA eng
NO The research leading to these results has received funding from the European Research Council under the European Union's Seventh Framework Programme (ERC grant agreement n° 338133)
NO Unión Europea. FP7
NO National Institute of General Medical Sciences (NHI)
DS Docta Complutense
RD 12 may 2025