The golgin family exhibits a propensity to form condensates in living cells.

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.

Ziltener P ，Rebane AA ，Graham M ，Ernst AM ，Rothman JE ... -  《-》

Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN.

Derby MC ，van Vliet C ，Brown D ，Luke MR ，Lu L ，Hong W ，Stow JL ，Gleeson PA ... -  《JOURNAL OF CELL SCIENCE》

Liquid-liquid phase separation of the Golgi matrix protein GM130.

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.

Rebane AA ，Ziltener P ，LaMonica LC ，Bauer AH ，Zheng H ，López-Montero I ，Pincet F ，Rothman JE ，Ernst AM ... -  《-》

Spatial proteomics defines the content of trafficking vesicles captured by golgin tethers.

Shin JJH ，Crook OM ，Borgeaud AC ，Cattin-Ortolá J ，Peak-Chew SY ，Breckels LM ，Gillingham AK ，Chadwick J ，Lilley KS ，Munro S ... -  《Nature Communications》

The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure.

Derby MC ，Lieu ZZ ，Brown D ，Stow JL ，Goud B ，Gleeson PA ... -  《TRAFFIC》