Liquid–liquid phase separation of the Golgi matrix protein GM130

Rebane, Aleksander A.; Ziltener, Pascal; LaMonica, Lauren C.; Bauer, Antonia H.; Zheng, Hong; López‐Montero, Iván; Pincet, Frédéric; Rothman, James E.; Ernst, Andreas

doi:10.1002/1873-3468.13715

Cited by 64 publications

(56 citation statements)

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“…Further, it has been shown that this relocation and assembly of the Golgi is dependent on the interaction of golgin160 with the minus‐end‐directed motor dynein, also implicating a specific golgin in the reassembly process [9]. We recently reported that the golgin GM130 phase separates into liquid‐like condensates both in vitro and in vivo [10], directly supporting the view that golgins can self‐assemble.…”

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confidence: 70%

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

et al. 2020

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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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confidence: 70%

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

et al. 2020

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“…Interactions with ELKS2 or other active zone proteins, some of which undergo phase separation as well ( Wu et al, 2019 ), may further account for the dynamic nature of vesicle clustering and vesicle progression toward release sites. Interestingly, even Golgins form liquid-phase condensates ( Rebane et al, 2020 ), and liquid-liquid-phase separation may be an organizational principle for vesicle tethering in the Golgi apparatus. Ultimately, an overarching and speculative model arises in which phase separation is a general mechanism through which vesicle tethering and traffic is organized throughout cells.…”

Section: Discussionmentioning

confidence: 99%

ELKS1 Captures Rab6-Marked Vesicular Cargo in Presynaptic Nerve Terminals

2020

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SUMMARY Neurons face unique transport challenges. They need to deliver cargo over long axonal distances and to many presynaptic nerve terminals. Rab GTPases are master regulators of vesicular traffic, but essential presynaptic Rabs have not been identified. Here, we find that Rab6, a Golgi-derived GTPase for constitutive secretion, associates with mobile axonal cargo and localizes to nerve terminals. ELKS1 is a stationary presynaptic protein with Golgin homology that binds to Rab6. Knockout and rescue experiments for ELKS1 and Rab6 establish that ELKS1 captures Rab6 cargo. The ELKS1-Rab6-capturing mechanism can be transferred to mitochondria by mistargeting ELKS1 or Rab6 to them. We conclude that nerve terminals have repurposed mechanisms from constitutive exocytosis for their highly regulated secretion. By employing Golgin-like mechanisms with anchored ELKS extending its coiled-coils to capture Rab6 cargo, they have spatially separated cargo capture from fusion. ELKS complexes connect to active zones and may mediate vesicle progression toward release sites.

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“…As such, the effect of unlinking is not caused by GRASP55 or 65 depletion alone, arguing that the structural effect is indirect. Consistent with this notion, GM130 has recently been shown to self-organize by liquid-liquid phase separation (Rebane et al, 2020), which might be a mechanism to assemble and maintain the matrix by including other Golgi proteins into the condensate.…”

Section: Discussionmentioning

confidence: 72%

Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure

Zhang

Seemann

2020

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AbstractGRASP65 and GRASP55 have been implicated in stacking of Golgi cisternae and lateral linking of stacks within the Golgi ribbon. However, loss of gene function approaches by RNAi or gene knockout to dissect their respective roles often resulted in conflicting conclusions. Here, we gene-edited GRASP55 and/or GRASP65 with a degron tag in human fibroblasts, allowing for the induced rapid degradation by the proteasome. We show that acute depletion of either GRASP55 or GRASP65 does not affect the Golgi ribbon, while chronic degradation of GRASP55 disrupts lateral connectivity of the Golgi ribbon. Acute double depletion of both GRASPs coincides with the loss of the vesicle tethering proteins GM130, p115 and Golgin-45 from the Golgi and compromises ribbon linking. Furthermore, neither GRASP55 and/or GRASP65 are required for maintaining stacks or de novo assembly of stacked cisternae at the end of mitosis. These results demonstrate that both GRASPs are dispensable for Golgi stacking, but are involved in maintaining the integrity of Golgi ribbon together with GM130 and Golgin-45.

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Liquid–liquid phase separation of the Golgi matrix protein GM130

Cited by 64 publications

References 40 publications

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

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

ELKS1 Captures Rab6-Marked Vesicular Cargo in Presynaptic Nerve Terminals

Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure

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