Katherine E Ward's research while affiliated with University of Notre Dame and other places

... Our investigation revealed significant findings for giant unilamellar vesicles (GUVs) incorporating saturated C1P species, notably C1P16, previously documented to induce gel domains 13,30 . The introduction of fluorescently tagged C1P16 has been shown to enhance rigidity and order within the lipid bilayer 31 . Unlike prior observations, autocorrelation curve morphology implies the presence of dual populations, possibly reflecting fluid and gel phases (Fig. S4). ...

... This protein is present on the exosome membrane surface and can combine with S100 (which is known to locate on the cell surface) to form a tetramer. This enhances ceramide-1-phosphate-dependent vascular endothelial cell invasion, which is thought to allow melanoma cells to hijack the exosomal transport of annexins to promote invasion [80][81][82][83][84]. ...

... We did not observe mPFN insertions into the membrane below the hydrophilic heads of POPC. Shallow membrane insertions were also observed in MD simulations of some other C2-domain-containing proteins, such as cytosolic phospholipase A2, PKCa, and synaptotagmin (48,49). PFN maintained an upright orientation during the simulation (120 ns in total) ( Figure 3). ...

... Traditionally, the induction of necrosis by anticancer compounds has been considered as an undesired event in the development of new drugs as it is an uncontrolled way leading to cell death, generally related to extreme conditions that could damage healthy tissues producing important side effects. However, triggering a regulated form of necrosis, i.e. necroptosis, has been described recently as an efficient MoA of some new anticancer drugs [40,41]. This novel paradigm for cytotoxic induction opened the door for alternative ways that could overcome resistance. ...

... With respect to their molecular mechanisms of action, there is a consensus that upon binding Ca 2+ , the C2-domains of syt1 and syt7 partially penetrate membranes that harbor anionic phospholipids 34,35 . This membrane penetration step might serve to destabilize the local phospholipid environment by introducing volume into the bilayer, buckling the membrane, and lowering the energy barrier for fusion 34,[36][37][38][39] . Additionally, membrane penetration could enable syts to regulate SNARE complex assembly 40,41 and stabilize curved intermediate structures 42 . ...

... We have demonstrated the mechanism and importance of the localization of PKC to the cSMAC region of the IS by showing that the V3 (hinge) region between the regulatory and catalytic domains of PKC binds to the cytoplasmic tail of CD28, likely through the kinase Lck, and this association is critical for the downstream functions of PKC in T cells (31). We also demonstrated that, similar to its nearest relative within the PKC family, PKC (35), the N-terminal C2-like domain of PKC is a phosphotyrosine (pTyr)binding domain (36). Nevertheless, the biological relevance of this function of PKC, as well as the identity of the pTyr-containing proteins that associate with the PKC C2 domain in TCR-stimulated T cells, remains to be determined. ...

... Cer can induce cell apoptosis by inhibiting mitochondrial electron transport and triggering the release of cytochrome C. Cytochrome C then activates caspase 3, initiating a cascade of events leading to cell death [114]. Additionally, ceramide kinase can convert Cer to ceramide-1-phosphate (C1P), which may contribute to inflammation by inhibiting tumor necrosis factor-α (TNF-α) signaling [115]. In contrast to the detrimental effects of ceramides, S1P acts as an anti-inflammatory, anti-apoptotic, and pro-proliferative signaling molecule. ...