Phosphoinositide kinase signaling controls ER-PM cross-talk

Omnus, Deike J.; Manford, Andrew G.; Bader, Jakob; Emr, Scott D.; Stefan, Christopher J.

doi:10.1091/mbc.e16-01-0002

Cited by 64 publications

(94 citation statements)

References 42 publications

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“…PI4P and PI(4,5)P2 metabolism control TORC2 signaling in budding yeast42. Compared to control cells, Gad8-S546 phosphorylation recovery in glucose starved cells transferred to glucose-rich medium was defective in its3-1 cells (Fig.…”

Section: Resultsmentioning

confidence: 93%

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Multiple crosstalk between TOR and the cell integrity MAPK signaling pathway in fission yeast

Madrid

Vázquez-Marín

Franco

et al. 2016

Sci Rep

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In eukaryotic cells, the highly conserved Target of Rapamycin (TOR) and the Mitogen Activated Protein Kinase (MAPK) signaling pathways elicit adaptive responses to extra- and intracellular conditions by regulating essential cellular functions. However, the nature of the functional relationships between both pathways is not fully understood. In the fission yeast Schizosaccharomyces pombe the cell integrity MAPK pathway (CIP) regulates morphogenesis, cell wall structure and ionic homeostasis. We show that the Rab GTPase Ryh1, a TORC2 complex activator, cross-activates the CIP and its core member, the MAPK Pmk1, by two distinct mechanisms. The first one involves TORC2 and its downstream effector, Akt ortholog Gad8, which together with TORC1 target Psk1 increase protein levels of the PKC ortholog Pck2 during cell wall stress or glucose starvation. Also, Ryh1 activates Pmk1 in a TORC2-independent fashion by prompting plasma membrane trafficking and stabilization of upstream activators of the MAPK cascade, including PDK ortholog Ksg1 or Rho1 GEF Rgf1. Besides, stress-activated Pmk1 cross-inhibits Ryh1 signaling by decreasing the GTPase activation cycle, and this ensures cell growth during alterations in phosphoinositide metabolism. Our results reveal a highly intricate cross-regulatory relationship between both pathways that warrants adequate cell adaptation and survival in response to environmental changes.

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Section: Resultsmentioning

confidence: 93%

“…8). In budding yeast, PI kinases may regulate PDK orthologs Pkh1/2 and TORC2 at the plasma membrane42. Hence, this dual functional role of PI kinases might be evolutionary conserved.…”

Section: Discussionmentioning

confidence: 99%

Multiple crosstalk between TOR and the cell integrity MAPK signaling pathway in fission yeast

Madrid

Vázquez-Marín

Franco

et al. 2016

Sci Rep

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“…Alternatively, since the ER is the site of lipid synthesis, it is possible that ER stress affects the production of certain lipid classes, leading to altered lipid asymmetry. It was recently reported that sphingolipid synthesis is altered in ∆tether cells [35]. Sphingolipids are mostly confined to the extracellular leaflet of the PM lipid bilayer, and thus contribute to generation of asymmetry in the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, it was reported that synthesis of sphingolipids, one of the major lipids in the PM, was reduced in ∆tether cells [35]. Sphingolipids are mostly confined to the outer leaflet of the PM, and thus contribute to the generation of lipid asymmetry.…”

Section: Impaired Complex Sphingolipid Synthesis Activates the Rim101mentioning

confidence: 99%

The Rim101 pathway contributes to ER stress adaptation through sensing the state of plasma membrane

Obara

Kihara

2016

Biochemical Journal

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Abbreviation list: DMSO, dimethyl sulfoxide; ER, endoplasmic reticulum; ESCRT, endosomal sorting complex required for transport; PM, plasma membrane; PtdSer, phosphatidylserine; Rim21C, C-terminal cytosolic region of Rim21; WT, wild-type 2 Summary statementThe sensor protein for plasma membrane lipid asymmetry, Rim21, detects ER stress by sensing alterations in the state of the plasma membrane, and triggers an adaptation response via the Rim101 pathway. 3 AbstractYeast cells sense alterations in the plasma membrane (PM) lipid asymmetry and external alkalization by the sensor protein Rim21, which functions in the Rim101 pathway. Rim101 signaling is initiated at the PM by the recruitment of the Rim101 signaling complex. The PM physically associates with the cortical endoplasmic reticulum (ER) to form ER-PM contact sites, where several signaling events, lipid exchange, and ion transport take place. In the present study, we investigated the spatial relationship between ER-PM contact sites and the sites of Rim101 signaling. Rim101 signaling mostly proceeds outside

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“…Thus, while it was reported that E-Syt2 is required for rapid endocytosis and signaling of growth factor receptors, including Fibroblast Growth Factor (FGF) receptor, such role is clearly dispensable in live animals [38–40]. Interestingly, however, tricalbin deficient yeast cells exhibit enhanced fragility upon heat-induced PM damage [41], and plant cells lacking E-Syt homologs show reduced tolerance to freezing [42, 43] and mechanical stress [44]. These findings suggest that absence of these proteins lead to altered biophysical properties of the PM, possibly as a result of an abnormal lipid composition of this membrane.…”

Section: Open Questionsmentioning

confidence: 99%

The Extended-Synaptotagmins

Saheki

Camilli

2017

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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The extended-synaptotagmins (tricalbins in yeast) derive their name from their partial domain structure similarity to the synaptotagmins, which are characterized by an N-terminal membrane anchor and cytosolically exposed C2 domains. However, they differ from the synaptotagmins in localization and function. The synaptotagmins tether secretory vesicles, including synaptic vesicles, to the plasma membrane (PM) via their C2 domains and regulate their Ca2+ triggered exocytosis. In contrast, the extended-synaptotagmins are resident proteins of the endoplasmic reticulum (ER), which tether this organelle to the plasma membrane via their C2 domains, but not as a premise to fusion of the two membranes. They transport glycerolipids between the two bilayers via their lipid-harboring SMP domains and Ca2+ regulate their membrane tethering and lipid transport function. Additionally, the extended-synaptotagmins are more widely expressed in different organisms, as they are present not only in animal cells, but also in fungi and plants, which do not express the synaptotagmins. Thus, they have a more general function than the synaptotagmins, whose appearance in animals species correlated with the occurrence of Ca2+ triggered exocytosis.

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Phosphoinositide kinase signaling controls ER-PM cross-talk

Cited by 64 publications

References 42 publications

Multiple crosstalk between TOR and the cell integrity MAPK signaling pathway in fission yeast

Multiple crosstalk between TOR and the cell integrity MAPK signaling pathway in fission yeast

The Rim101 pathway contributes to ER stress adaptation through sensing the state of plasma membrane

The Extended-Synaptotagmins

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