Eisosomes Regulate Phosphatidylinositol 4,5-Bisphosphate (PI(4,5)P2) Cortical Clusters and Mitogen-activated Protein (MAP) Kinase Signaling upon Osmotic Stress

Kabeche, Ruth; Madrid, Marisa; Cansado, José; Moseley, James B.

doi:10.1074/jbc.m115.674192

Cited by 30 publications

(20 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both Ksg1 and Rgf1 harbor phosphoinositide-binding pleckstrin homology (PH) domains at their C-termini, and Rgf1 localization at cell tips is diminished in cells expressing a thermosensitive its3-1 allele40. Importantly, and similar to ryh1∆ cells, Pmk1 activation induced by salt stress is also impaired in its3-1 cells41. As shown in Fig.…”

Section: Resultsmentioning

confidence: 87%

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

Madrid

Vázquez-Marín

Franco

et al. 2016

Sci Rep

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 87%

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

Madrid

Vázquez-Marín

Franco

et al. 2016

Sci Rep

Self Cite

View full text Add to dashboard Cite

show abstract

“…Patches of PI 4,5 P 2 were detected in the plasma membrane of S. pombe and S. cerevisiae in response to osmotic stress, which might be related to the PI 4,5 P 2 patches seen in C. albicans sur7∆ and pil1∆ lsp1∆ mutants ( Kabeche et al. , 2015 ).…”

Section: Discussionmentioning

confidence: 97%

Eisosomes promote the ability of Sur7 to regulate plasma membrane organization inCandida albicans

Wang

Douglas

Veselá

et al. 2016

MBoC

View full text Add to dashboard Cite

show abstract

“…On the other hand, it has been reported previously that, instead, Inp51 is recruited to the PM via specific interaction with Tax4 (and its paralog Irs4), which are orthologs of mammalian EPS15 [ 90 ]. Similarly, in S. pombe , there is evidence that eisosomes are involved in regulating PM PtdIns4,5P2 levels [ 91 ] and localization [ 92 ].…”

Section: Structure Function and Regulation Of Ypk1mentioning

confidence: 99%

The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

et al. 2017

View full text Add to dashboard Cite

To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and master regulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: Ypk1 (mammalian ortholog is SGK1), along with a paralog (Ypk2); and, Pkc1 (mammalian ortholog is PKN2/PRK2). Ypk1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase Pkh1 (mammalian ortholog is PDK1) and a paralog (Pkh2). For cell survival under various stresses, Ypk1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. Pkc1 controls diverse processes, especially cell wall synthesis and integrity. Pkc1 is also regulated by Pkh1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by Ypk1-mediated and Pkc1-mediated phosphorylation.

show abstract

Eisosomes Regulate Phosphatidylinositol 4,5-Bisphosphate (PI(4,5)P2) Cortical Clusters and Mitogen-activated Protein (MAP) Kinase Signaling upon Osmotic Stress

Cited by 30 publications

References 53 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

Eisosomes promote the ability of Sur7 to regulate plasma membrane organization inCandida albicans

The TORC2‐Dependent Signaling Network in the Yeast Saccharomyces cerevisiae

Contact Info

Product

Resources

About