Golgi-Resident Gαo Promotes Protrusive Membrane Dynamics

Solis, Gonzalo P.; Bilousov, Oleksii; Koval, Alexey; Lüchtenborg, Anne-Marie; Chen, Lin; Katanaev, Vladimir L.

doi:10.1016/j.cell.2017.08.045

Cited by 13 publications

(10 citation statements)

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“…Deviations from perfect balance, if not sensed and corrected, would lead to rapid compositional and morphological disruption of this organelle [37,38]. Here, a control system senses the incoming fluxes using the KDEL-receptor as a sensor that detects arrival at the Golgi of a specific group of chaperones escaping the ER, and activates multiple signal transduction pathways to regulate the retrograde and anterograde export out of the Golgi and so counteract imbalances in the membrane/proteins content in the Golgi [37][38][39][40]. In more detail, the KDEL sequence-containing tail of chaperones binds the KDELR, thus stimulating the Golgi localized Gq [39] and Gs proteins [37].…”

Section: The Cis-golgi Kdelr-based Autoregulatory Systemmentioning

confidence: 99%

Regulation of cargo export and sorting at the trans‐Golgi network

2019

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The sorting and distribution to different final destinations of roughly a third of the membrane and secreted proteins occurs at the level of the trans‐Golgi network (TGN). This TGN mission involves efficient mechanisms of cargo recognition and activation of specific signalling pathways. This is important because protein localization is strictly connected with function, and many aberrant phenotypes may occur when a protein is missorted to the wrong cellular compartment. In this review, we briefly summarize the principal players known to be involved in TGN functions, highlighting the importance of regulatory signalling pathways and also the pathological outcomes of aberrant sorting and export events from the TGN compartment.

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Section: The Cis-golgi Kdelr-based Autoregulatory Systemmentioning

confidence: 99%

Regulation of cargo export and sorting at the trans‐Golgi network

2019

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“…al., 2014;Luini and Parashuraman, 2016) A well characterized homeostatic device is the unfolded protein response (UPR), which regulates the levels of unfolded proteins in the ER through multiple signaling and transcriptional cascades (Walter and Ron, 2011). Other examples are the autoregulatory systems that operate in the ER (Subramanian et al, 2019;Centonze et al, 2019) and the Golgi (Pulvirenti et al, 2008;Giannotta et al, 2012;Cancino et al, 2014;Solis et al, 2017;Tapia et al, 2019) that ensure the correct trafficking through these stations. So far, the organization, molecular determinants and function of a potential autoregulatory circuit at the TGN has not been examined.…”

Section: Introductionmentioning

confidence: 99%

Autoregulatory circuit regulating basolateral cargo export from the TGN: role of the orphan receptor GPRC5A in PKD signaling and cell polarity

Martino

Capalbo

Sticco

et al. 2020

Preprint

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The membrane transport apparatus comprises a series of separate membrane bound compartments, or transport stations, that are responsible for the synthesis, processing, transport, sorting and delivery to their final cellular destinations of most transmembrane and soluble lumenal proteins. Over the last decades the membrane transport system has been shown to be extensively regulated both by environmental inputs and by internal homeostatic signalling systems, or control systems, that operate to maintain the homeostasis and optimal functionality of the main transport stations, such as the endoplasmic reticulum and the Golgi, in the face of internal and external perturbations. The trans-Golgi network (TGN) is a major transport and processing station and the main sorting compartment of the transport apparatus. However, the mechanisms that control cargo export and sorting at the TGN have so far remained elusive. Here we focus on the sorting of basolateral cargo proteins and show that these proteins bind to the TGN localized orphan receptor GPRC5A. The cargo-GPRC5A complex triggers the activation of a signaling pathway that involves the Gβγ subunits dependent activation of the phospholipase C beta 3 (PLCβ3), which inturn induces diacyl glycerol (DAG) production. DAG recruits and activates protein kinase D (PKD) and the phosphorylation of its substrates. This step results in the formation of basolateral carriers for delivery of these cargoes to the basolateral plasma membrane domain. We term this mechanism "ARTG" (AutoRegulation of TGN export). Remarkably, the impairment of ARTG pathway components, and in particular of GPRC5A, causes defects in the polarized organization of epithelial cells.

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“…Further studies in plants are neededto investigate how the inhibitory effect of plant heterotrimeric G protein complex on ERD2s was regulated by the incoming cargos. A recent report suggested mammalian ERD2 binds and activates monomeric Gαo, and Gαo which can then interact with GTPases Rab1 and Rab3 to promote the transport from Golgi to PM (Solis et al ), and the inhibition of ER retention by depletion of p24 proteins causes the secretion of BiP to the apoplast in Arabidopsis (Pastor‐Cantizano et al ). Consistent with these findings, we showed that G protein subunits interacted with ERD2s and silencing of G protein subunits inhibited the secretion of HDEL cargo (Figure S7B).…”

Section: Discussionmentioning

confidence: 99%

“…Besides their role in ER retrieval, mammalian ERD2s can modulate ER stress responses through mitogen‐activated protein kinase (MAPK) signaling cascades and activate Src family kinases in the Golgi complex to regulate Golgi‐to‐plasma membrane transport (Aoe et al ; Yamamoto et al ; Pulvirenti et al ). Recently, a mammalian KDEL receptor (mammalian ERD2) was reported to activate the heterotrimeric G protein alpha subunit, Ga q/11 or monomeric Gαo and, in turn, promoted protein forward transport from the Golgi to the plasma membrane (Giannotta et al ; Solis et al ).…”

Section: Introductionmentioning

confidence: 99%

Plant G proteins interact with endoplasmic reticulum luminal protein receptors to regulate endoplasmic reticulum retrieval

Wang

Xie

et al. 2018

JIPB

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Maintaining endoplasmic reticulum (ER) homeostasis is essential for the production of biomolecules. ER retrieval, i.e., the retrograde transport of compounds from the Golgi to the ER, is one of the pathways that ensures ER homeostasis. However, the mechanisms underlying the regulation of ER retrieval in plants remain largely unknown. Plant ERD2-like proteins (ERD2s) were recently suggested to function as ER luminal protein receptors that mediate ER retrieval. Here, we demonstrate that heterotrimeric G protein signaling is involved in ERD2-mediated ER retrieval. We show that ERD2s interact with the heterotrimeric G protein Ga and Gg subunits at the Golgi.

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Golgi-Resident Gαo Promotes Protrusive Membrane Dynamics

Cited by 13 publications

References 0 publications

Regulation of cargo export and sorting at the trans‐Golgi network

Regulation of cargo export and sorting at the trans‐Golgi network

Autoregulatory circuit regulating basolateral cargo export from the TGN: role of the orphan receptor GPRC5A in PKD signaling and cell polarity

Plant G proteins interact with endoplasmic reticulum luminal protein receptors to regulate endoplasmic reticulum retrieval

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