Signalling to and from the secretory pathway

Farhan, Hesso; Rabouille, Cathérine

doi:10.1242/jcs.076455

Cited by 131 publications

(93 citation statements)

References 98 publications

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“…Targeting these central organelles is likely the most effective way of shutting down the entire protein distribution system as they are at the confluent of many routes. In addition, the Golgi and endosomes are recognized as signaling hubs, which are not only able to respond to environmental factors but are also able to modulate the outcome of signaling cascades by housing signaling molecules [140,141]. Therefore, an attractive possibility is that trafficking alteration induced by caspases may also initiate specific signaling events at these two organelles.…”

Section: Discussionmentioning

confidence: 99%

Caspases rule the intracellular trafficking cartel

2017

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During apoptosis, caspases feast on several hundreds of cellular proteins to orchestrate rapid cellular demise. Indeed, caspases are known to get a taste of every cellular process in one way or another, activating some, but most often shutting them down. Thus, it is not surprising that caspases proteolyze proteins involved in intracellular trafficking with particularly devastating consequences for this important process. This review article focuses on how caspases target the machinery responsible for smuggling goods within and outside the cell.

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Section: Discussionmentioning

confidence: 99%

Caspases rule the intracellular trafficking cartel

2017

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“…A number of studies have implicated MEK-ERK in the regulation of vesicle trafficking (reviewed in ref. 39). For exocytosis, it was recently shown that ERK1/2 phosphorylate the exocyst subunit Exo70 and promote exocyst complex assembly (23).…”

Section: Discussionmentioning

confidence: 99%

Activation of Rab8 guanine nucleotide exchange factor Rabin8 by ERK1/2 in response to EGF signaling

Wang

Ren

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Exocytosis is tightly regulated in many cellular processes, from neurite expansion to tumor proliferation. Rab8, a member of the Rab family of small GTPases, plays an important role in membrane trafficking from the trans-Golgi network and recycling endosomes to the plasma membrane. Rabin8 is a guanine nucleotide exchange factor (GEF) and major activator of Rab8. Investigating how Rabin8 is activated in cells is thus pivotal to the understanding of the regulation of exocytosis. Here we show that phosphorylation serves as an important mechanism for Rabin8 activation. We identified Rabin8 as a direct phospho-substrate of ERK1/2 in response to EGF signaling. At the molecular level, ERK phosphorylation relieves the autoinhibition of Rabin8, thus promoting its GEF activity. We further demonstrate that blocking ERK1/2-mediated phosphorylation of Rabin8 inhibits transferrin recycling to the plasma membrane. Together, our results suggest that ERK1/2 activate Rabin8 to regulate vesicular trafficking to the plasma membrane in response to extracellular signaling.Rab GTPases | Rab8 | guanine nucleotide exchange factor | ERK | phosphorylation

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“…COPII-mediated ER export, from coat recruitment to vesicle scission, depends on the membrane composition, not only of proteins but also lipids (Blumental-Perry et al, 2006;Farhan and Rabouille, 2011;Miller and Barlowe, 2010;Shindiapina and Barlowe, 2010). Yeast cells lacking Osh proteins or both Scs2p and Scs22p accumulate PtdIns4P (Stefan et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast

Kajiwara

Ikeda

Aguilera-Romero

et al. 2013

Journal of Cell Science

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Lipids synthesized at the endoplasmic reticulum (ER) are delivered to the Golgi by vesicular and non-vesicular pathways. ER-to-Golgi transport is crucial for maintaining the different membrane lipid composition and identities of organelles. Despite their importance, mechanisms regulating transport remain elusive. Here we report that in yeast coat protein complex II (COPII) vesicle-mediated transport of ceramide from the ER to the Golgi requires oxysterol-binding protein homologs, Osh proteins, which have been implicated in lipid homeostasis. Because Osh proteins are not required to transport proteins to the Golgi, these results indicate a specific requirement for the Osh proteins in the transport of ceramide. In addition, we provide evidence that Osh proteins play a negative role in COPII vesicle biogenesis. Together, our data suggest that ceramide transport and sphingolipid levels between the ER and Golgi are maintained by two distinct functions of Osh proteins, which negatively regulate COPII vesicle formation and positively control a later stage, presumably fusion of ceramide-enriched vesicles with Golgi compartments.

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Signalling to and from the secretory pathway

Cited by 131 publications

References 98 publications

Caspases rule the intracellular trafficking cartel

Caspases rule the intracellular trafficking cartel

Activation of Rab8 guanine nucleotide exchange factor Rabin8 by ERK1/2 in response to EGF signaling

Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast

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