Stressors ranging from nutrient deprivation to immune signaling can induce the degradation of cytoplasmic material by a process known as autophagy. Increasingly, research on autophagy has begun to focus on its role in inflammation and the immune response. Autophagy acts as an immune effector that mediates pathogen clearance. The roles of autophagy bridge both the innate and adaptive immune systems and include functions in thymic selection, antigen presentation, promotion of lymphocyte homeostasis and survival, and regulation of cytokine production. In this review, we discuss the mechanisms by which autophagy is regulated, as well as the functions of autophagy and autophagy proteins in immunity and inflammation.
We have controllably modulated the drain current (I(D)) and threshold voltage (V(T)) in pseudo metal-oxide-semiconductor field-effect transistors (MOSFETs) by grafting a monolayer of molecules atop oxide-free H-passivated silicon surfaces. An electronically controlled series of molecules, from strong pi-electron donors to strong pi-electron acceptors, was covalently attached onto the channel region of the transistors. The device conductance was thus systematically tuned in accordance with the electron-donating ability of the grafted molecules, which is attributed to the charge transfer between the device channel and the molecules. This surface grafting protocol might serve as a useful method for controlling electronic characteristics in small silicon devices at future technology nodes.
Peptide metabolism is a complex process involving many proteins working in concert. Mass spectrometry (MS)-based global peptide profiling of mice lacking dipeptidyl peptidase 4 (DPP4) identified endogenous DPP4 substrates and revealed an unrecognized pathway during proline peptide catabolism that interlinks aminopeptidase and DPP4 activities. Together, these studies elucidate specific aspects of DPP4-regulated metabolism and, more generally, highlight the utility of global peptide profiling for studying peptide metabolism in vivo.
We report that 4-(3-(benzyloxy)phenyl)-2-ethylsulfinyl-6-(trifluoromethyl)pyrimidine (BETP), which behaves as a positive allosteric modulator at the glucagon-like peptide-1 receptor (GLP-1R), covalently modifies cysteines 347 and 438 in GLP-1R. C347, located in intracellular loop 3 of GLP-1R, is critical to the activity of BETP and a structurally distinct GLP-1R ago-allosteric modulator, N-(tert-butyl)-6,7-dichloro-3-(methylsulfonyl)quinoxalin-2-amine. We further show that substitution of cysteine for phenylalanine 345 in the glucagon receptor is sufficient to confer sensitivity to BETP.
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