2026-06-27T10:21:36Zhttps://docta.ucm.es/rest/oai/requestoai:docta.ucm.es:20.500.14352/61832023-08-04T02:33:21Zcom_20.500.14352_14col_20.500.14352_15
Docta Complutense
author
Rebane, Aleksander A.
author
Ziltener, Pascal
author
LaMonica, Lauren C.
author
Bauer, Antonia H.
author
Zheng, Hong
author
López-Montero, Iván
author
Pincet, Frederic
author
Rothman, James E.
author
Ernst, Andreas M.
2023-06-16T15:17:12Z
2023-06-16T15:17:12Z
2020
0014-5793
10.1002/1873-3468.13715
https://hdl.handle.net/20.500.14352/6183
https://doi.org/10.1002/1873-3468.13715
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.
eng
Atribución 3.0 España
Liquid–liquid phase separation of the Golgi matrix protein GM130
journal article
URL
https://docta.ucm.es/bitstreams/11c3e4d2-eea3-4891-96d0-150cb977999d/download
File
MD5
e05d36cefa303422177e438285f55255
1730781
application/pdf
1873-3468.13715.pdf