Control Systems of Membrane Transport at the Interface between the Endoplasmic Reticulum and the Golgi

Cancino, Jorge; Capalbo, Anita; Campli, Antonella Di; Giannotta, Monica; Rizzo, Riccardo; Jung, Juan E.; Martino, Rosaria Di; Persico, Maria; Heinklein, Petra; Sallese, Michele; Luini, Alberto

doi:10.1016/j.devcel.2014.06.018

Cited by 101 publications

(162 citation statements)

References 93 publications

(126 reference statements)

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“…Interestingly, the retrograde transport of STxB-KDEL to the ER was not affected by PLCγ1 silencing (Figure S4). A recent study shows that cargo arrival at the Golgi activates Gs and PKA through KDEL receptor to promote retrograde transport to the ER (22). This finding, together with our results, suggests that cargo arrival can trigger different signalling pathways to induce the different routes to exit the Golgi, such as KDELR-Gs-PKA for the retrograde transport to the ER and PLCγ1-DAG-PKD for the post-Golgi trafficking.…”

Section: Discussionsupporting

confidence: 84%

PLCγ1 Participates in Protein Transport and Diacylglycerol Production Triggered by cargo Arrival at the Golgi

Sicart

Katan

Egea

et al. 2015

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Diacylglycerol (DAG) is required for membrane traffic and structural organization at the Golgi. DAG is a lipid metabolite of several enzymatic reactions present at this organelle, but the mechanisms by which they are regulated are still unknown. Here, we show that cargo arrival at the Golgi increases the recruitment of the DAG-sensing constructs C1-PKCθ-GFP and the PKD-wt-GFP. The recruitment of both constructs was reduced by PLCγ1 silencing. Post-Golgi trafficking of transmembrane and soluble proteins was impaired in PLCγ1-silenced cells. Under basal conditions, PLCγ1 contributed to the maintenance of the pool of DAG associated with the Golgi and to the structural organization of the organelle. Finally, we show that cytosolic phospholipase C (PLC) can hydrolyse phosphatidylinositol 4-phosphate in isolated Golgi membranes. Our results indicate that PLCγ1 is part of the molecular mechanism that couples cargo arrival at the Golgi with DAG production to co-ordinate the formation of transport carriers for post-Golgi traffic.

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Section: Discussionsupporting

confidence: 84%

PLCγ1 Participates in Protein Transport and Diacylglycerol Production Triggered by cargo Arrival at the Golgi

Sicart

Katan

Egea

et al. 2015

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“…Fragmented Golgi membranes with shorter cisternae stacks were also evident (Figure 1b,c). The observed defects in the ER and Golgi organization is consistent with a defect in ER/Golgi trafficking (Cancino et al, 2014;Vollrath et al, 2014;Zhao et al, 2015).…”

Section: R E Sults An D Discussionsupporting

confidence: 79%

ER/Golgi trafficking is facilitated by unbranched actin filaments containing Tpm4.2

et al. 2017

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We have identified novel actin filaments defined by tropomyosin Tpm4.2 at the ER. EM analysis of mouse embryo fibroblasts (MEFs) isolated from mice expressing a mutant Tpm4.2 (Tpm4 ), incapable of incorporating into actin filaments, revealed swollen ER structures compared with wild-type (WT) MEFs (Tpm4 ). ER-to-Golgi, but not Golgi-to-ER trafficking was altered in the Tpm4 MEFs following the transfection of the temperature sensitive ER-associated ts045-VSVg construct. Exogenous Tpm4.2 was able to rescue the ER-to-Golgi trafficking defect in the Tpm4 cells. The treatment of WT MEFs with the myosin II inhibitor, blebbistatin, blocked the Tpm4.2-dependent ER-to-Golgi trafficking. The lack of an effect on ER-to-Golgi trafficking following treatment of MEFs with CK666 indicates that branched Arp2/3-containing actin filaments are not involved in anterograde vesicle trafficking. We propose that unbranched, Tpm4.2-containing filaments have an important role in maintaining ER/Golgi structure and that these structures, in conjunction with myosin II motors, mediate ER-to-Golgi trafficking.

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“…Considering the longrecognized importance of GPCR-G protein signal termination at the plasma membrane (7,8), this would seem a critical future direction. Yet another interesting direction is toward investigating broader implications of endomembrane G protein activation, such as its recently proposed role in homeostatic control of the biosynthetic pathway by the seven-transmembrane KDEL cargo receptor through receptor-mediated activation of G s in the Golgi apparatus (60).…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

G Protein-coupled Receptor (GPCR) Signaling via Heterotrimeric G Proteins from Endosomes

Tsvetanova¹,

Irannejad²,

Zastrow

2015

Journal of Biological Chemistry

141

122

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Some G protein-coupled receptors (GPCRs), in addition to activating heterotrimeric G proteins in the plasma membrane, appear to elicit a "second wave" of G protein activation after ligand-induced internalization. We briefly summarize evidence supporting this view and then discuss what is presently known about the functional significance of GPCR-G protein activation in endosomes. Endosomal activation can shape the cellular response temporally by prolonging its overall duration, and may shape the response spatially by moving the location of intracellular second messenger production relative to effectors.It has been more than 20 years since regulated endocytosis of GPCRs 3 through ligand-dependent concentration in coated pits was established (1, 2). Much has been learned since that time about the large number of GPCRs that engage this cellular regulatory mechanism, its biochemical underpinnings, and later events determining receptor-specific trafficking itineraries. However, our understanding of how endocytosis impacts canonical G protein-dependent signaling has remained unchanged. Fundamental to this paradigm is the belief that receptor-mediated activation of cognate heterotrimeric G proteins is restricted to the plasma membrane, and that internalized receptors are effectively silent with regard to this transduction mechanism.Evidence accumulated over the past several years is beginning to challenge this view. Here we summarize data supporting an alternative hypothesis, that endosomes represent dynamic sites of GPCR-G protein activation. We then focus on what is beginning to be learned about the functional significance of the endosome signal, limiting scope to the relatively few GPCRs for which relevant data are presently available. When one considers this limitation, together with the remarkable diversity of membrane trafficking properties that distinguish even very similar GPCR homologs (e.g. Ref.3) and splice variants (e.g. Ref. 4), it seems likely that much more remains to be learned.

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Control Systems of Membrane Transport at the Interface between the Endoplasmic Reticulum and the Golgi

Cited by 101 publications

References 93 publications

PLCγ1 Participates in Protein Transport and Diacylglycerol Production Triggered by cargo Arrival at the Golgi

PLCγ1 Participates in Protein Transport and Diacylglycerol Production Triggered by cargo Arrival at the Golgi

ER/Golgi trafficking is facilitated by unbranched actin filaments containing Tpm4.2

G Protein-coupled Receptor (GPCR) Signaling via Heterotrimeric G Proteins from Endosomes

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