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• W2767906974 abstract "2) the SIKE:tubulin interaction may be sensitive to SIKE’s phosphorylation state, 3) the SIKE:alpha‐actinin interaction is unaffected by SIKE phosphorylation, and 4) the SIKE:tubulin interaction is direct. Together, MOLECULAR BIOLOGY OF THE CELL these studies establish an interaction between SIKE and cytoskeletal proteins that may provide a direct Volume: 27 Mee8ng Abstract: P2189 link between innate immune signaling and cytoskeletal components. Work supported by NIH grant R21AI107447. Published: POSTER PRESENTATIONS‐ TUESDAY P2189 Board Number: B1116 P2188 Novel insights into regulation of Target of Rapamycin Complex 2 by hyperosmotic stress. Board Number: B1115 K.L. Leskoske , F.M. Roelants , J.W. Thorner Suppressor of IKK epsilon (SIKE) links the cytoskeleton to innate immune signaling pathways. Department of Molecular Cell Biology, University of California, Berkeley, Berkeley, CA H.A. Sonnenschein , F. Slykas 1 , K.F. Lawrence 2 , J.K. Bell 1 ; Chemistry Biochemistry Department, University of San Diego, San Diego, CA, 2 Immunology Target of Rapamycin (TOR) Complex 2 (TORC2) is a multi‐subunit protein kinase associated with the Microbiology Department, Virginia Commonwealth University, Richmond, VA plasma membrane that is an essential regulator of growth. Ample genetic and biochemical evidence indicates that, in Saccharomyces cerevisiae, TORC2 exerts its effects solely via direct phosphorylation Innate immunity coordinates the first line of defense against invading pathogen. Innate immune POSTER PRESENTATIONS‐ TUESDAY and upregulation of the activity of the downstream protein kinase Ypk1 (and its paralog Ypk2). TORC2‐ receptors signal production of pro‐inflammatory, anti‐viral, and apoptotic responses. Signals coalesce at Ypk1 signaling, in turn, regulates various aspects of the lipid composition and organization of the plasma catalytic hubs, such as kinases, to amplify downstream signaling and act as key sites of regulation. In the membrane during normal cell growth. In addition, TORC2 activity, and thus Ypk1 function, is modulated anti‐viral response, TANK binding kinase 1 (TBK1) functions as a catalytic hub. Suppressor of IKK epsilon by environmental insults that exert stress on the plasma membrane. Ypk1 action maintains plasma (SIKE) was initially characterized as a negative regulator of TBK1‐mediated anti‐viral pathways. membrane homeostasis in multiple ways. For example, in response to sphingolipid depletion, TORC2 Subsequent study found SIKE acts as a high affinity, alternate TBK1 substrate, consistent with SIKE being activates Ypk1, which then phosphorylates targets that stimulate sphingolipid synthesis, inhibit phosphorylated upon viral infection. The goals of this project are to determine the function of SIKE and aminoglycero‐phospholipid flipping, and block endocytosis of integral plasma membrane proteins. In phosphorylated SIKE. The primary objective of this work was to examine the SIKE interaction network to contrast, in response to hyperosmotic shock, TORC2 stimulation of Ypk1 is rapidly lost, alleviating Ypk1‐ infer SIKE function. Tandem MS/MS of immunoprecipitated FLAG‐tagged SIKE from transiently‐ mediated inhibition of Gpd1‐dependent glycerol production and preventing Ypk1‐mediated opening of transfected cells revealed 27% of the SIKE interaction network consisted of actin and tubulin partners. the aquaglyceroporin Fps1, thereby allowing cells to rapidly accumulate intracellular glycerol to Using confocal microscopy, endogenous SIKE was shown to strongly colocalize with actin, tubulin, alpha‐ counteract the increase in extracellular tonicity. How hypertonic conditions influence TORC2 is not well actinin and to a lesser extent ezrin, focal adhesion kinase, and beta‐catenin. Structured illumination understood. We report here that the plasma membrane‐localized osmosensor Sln1 is an upstream microscopy showed that actin and alpha‐actinin maintained colocalization with SIKE. Reciprocal regulator of TORC2. Inactivation of Sln1, as occurs under hyperosmotic conditions, leads to loss of immunoprecipitation (RcIP) using GFP‐labeled actin or alpha‐actinin or DsRed‐tubulin with FLAG‐tagged TORC2 phosphorylation of Ypk1. Upon Sln1 inactivation, the TORC2 subunit Avo2 is phosphorylated at SIKE from transiently transfect cells indicated that the SIKE:actin interaction was not maintained under its MAPK phosphoacceptor sites. This response requires two mitogen (messenger)‐activated protein these conditions. The SIKE:tubulin interaction appeared enhanced upon stimulation with dsRNA, a kinases (MAPKs), Hog1 and Slt2/Mpk1. Absence of Avo2 partially restores TORC2‐mediated stimulation mimic of viral infection. The SIKE:alpha‐actinin interaction was neither disrupted nor enhanced by of Ypk1 under hyperosmotic conditions. These results suggest that the phosphorylation status of the stimulation. To determine if cytoskeletal proteins interacted directly with SIKE, in vitro precipitations Avo2 subunit of TORC2 serves as a rheostat for controlling TORC2 function. were completed using recombinant 6X‐His tagged SIKE and porcine tubulin (monomeric) or rabbit alpha‐ actinin. Lysozyme served as a negative control for non‐specific binding to SIKE. SIKE:target were P2190 incubated at 1:0.5, 1:1 and 1:1.4 molar ratios, precipitated using Ni‐NTA resin, and eluted proteins Board Number: B1117 assessed by SDS‐PAGE. SIKE:tubulin interactions were detected at all stoichiometries, whereas no Novel approach for rapid development of optimized FRET‐based biosensor for signaling SIKE:lysozyme interaction was observed. From these studies, 1) SIKE interacts with cytoskeletal proteins, 2) the SIKE:tubulin interaction may be sensitive to SIKE’s phosphorylation state, 3) the SIKE:alpha‐actinin network interrogation in cellulo and in vivo. interaction is unaffected by SIKE phosphorylation, and 4) the SIKE:tubulin interaction is direct. Together, F. Sipieter 1,2 , B. Cappe 1,2 , O.C. Gavet 3 , L. Heliot 4 , P. Vandenabeele 1,2 , P. Vincent 5 , F.B. Riquet 1,2,6 ; these studies establish an interaction between SIKE and cytoskeletal proteins that may provide a direct Molecular Signaling and Cell Death Unit, Department of Biomedical Molecular Biology, Ghent link between innate immune signaling and cytoskeletal components. Work supported by NIH grant University, Ghent, Belgium, 2 Molecular Signaling and Cell Death Unit, Inflammation Research Center R21AI107447. (IRC), a VIB‐UGent department, VIB, Ghent, Belgium, 3 Institut Gustave Roussy (IGR), CNRS‐UMR 8200, CNRS/Paris‐Sud University, Villejuif, France, 4 Team Biophotonique Cellulaire Fonctionnelle, Laboratoire P2189 de Physique des Lasers, Atomes et Molecules (PhLAM), CNRS UMR 8523, CNRS/Lille1 University, Villeneuve d’Ascq, France, Board Number: B1116 5 Neurobiologie des processus adaptatifs (NPA), CNRS UMR 7102, CNRS / UPMC Paris 6, Paris, France, 6 Structural and Functional Glycobiology Unit (UGSF), CNRS UMR 8576, Lille Novel insights into regulation of Target of Rapamycin Complex 2 by hyperosmotic stress. 1 University, Villeneuve d’Ascq, France K.L. Leskoske , F.M. Roelants , J.W. Thorner ; Department of Molecular Cell Biology, University of California, Berkeley, Berkeley, CA Towards comprehensive understanding of molecular signaling regulation at the single living cells level, biosensors provide a read‐out of biochemical events with a high spatiotemporal resolution. However, Target of Rapamycin (TOR) Complex 2 (TORC2) is a multi‐subunit protein kinase associated with the the recording of biochemical events during unperturbed cellular processes is challenged by biosensor plasma membrane that is an essential regulator of growth. Ample genetic and biochemical evidence sensitivity. To alleviate the problem, we propose a validated approach to accelerate the development indicates that, in Saccharomyces cerevisiae, TORC2 exerts its effects solely via direct phosphorylation for highly sensitive genetically encoded FRET biosensors. Considering the importance of kinases in the and upregulation of the activity of the downstream protein kinase Ypk1 (and its paralog Ypk2). TORC2‐" @default.
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• W2767906974 title "Novel insights into regulation of Target of Rapamycin Complex 2 by hyperosmotic stress." @default.
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