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• W3094256900 endingPage "250" @default.
• W3094256900 startingPage "238" @default.
• W3094256900 abstract "Bacteria have evolved diverse effector proteins that function as cysteine proteases to cause irreversible delipidation of host lipidated proteins, thereby resulting in disruption of the host's lipidated-protein-mediated-signaling landscape as a mechanism of microbial pathogenesis. Yersinia YopT releases Rho GTPases from the plasma membrane by cleaving S-prenylated cysteine residues at the C terminus, resulting in destruction of the actin cytoskeleton of host cells. Shigella IpaJ deconjugates the N-myristoylation modification from Golgi-associated Arf1 GTPase, thereby disrupting Golgi organization. Legionella RavZ irreversibly cleaves phosphatidylethanolamine (PE)-modified LC3 (LC3-PE) to inhibit autophagosome formation. The pathogen's effector-catalyzed host delipidation has a common concerted mechanism, with three key sequential steps – membrane targeting, substrate recognition, and proteolysis – to achieve their function. Protein lipidation, the covalent attachment of a lipid moiety to a target protein, plays a critical role in many cellular processes in eukaryotic cells. Bacterial pathogens secrete various effectors to subvert the host signaling pathway as a mechanism of microbial pathogenesis. An increasing number of effectors from diverse bacterial pathogens function as cysteine proteases to cause irreversible delipidation of host lipidated proteins. This in turn results in disruption of crucial lipidation-mediated host signal transduction, thereby enabling pathogen survival and replication. In this review, we discuss the role of the bacterial effectors in interactions with the host and highlight our knowledge of irreversible host delipidation, with a focus on the common concerted biochemical mechanisms of the bacterial effectors. Protein lipidation, the covalent attachment of a lipid moiety to a target protein, plays a critical role in many cellular processes in eukaryotic cells. Bacterial pathogens secrete various effectors to subvert the host signaling pathway as a mechanism of microbial pathogenesis. An increasing number of effectors from diverse bacterial pathogens function as cysteine proteases to cause irreversible delipidation of host lipidated proteins. This in turn results in disruption of crucial lipidation-mediated host signal transduction, thereby enabling pathogen survival and replication. In this review, we discuss the role of the bacterial effectors in interactions with the host and highlight our knowledge of irreversible host delipidation, with a focus on the common concerted biochemical mechanisms of the bacterial effectors. a class of proteins secreted by pathogens into the cells of their host using a secretion system. Effector proteins are usually critical for pathogenic virulence. a group of proteins with a specific amino acid sequence at the C terminus that directs their post-translational modification. C is a cysteine residue, aa are two aliphatic residues, and X represents any C-terminal amino acid depending on the substrate specificity. In the case of Rho GTPases, the CaaX Cys bears S-prenylation, and further endoproteolytic removal of the last three amino acids (aaX) by Rce1 (Ras-converting enzyme 1) and carboxy-terminal methyl ester of the S-prenylated cysteine by Icmt (isoprenylcysteine carboxyl methyltransferase) produces the fully functional Rho GTPases containing S-prenylated cysteine methyl ester residue. a set of three coordinated amino acids consisting of an acid residue, base residue, and nucleophile that are found in the active site of some enzymes involved in catalysis. The acid residue (commonly glutamate or aspartate) aligns and polarizes the base (usually histidine), which activates the nucleophile (often cysteine or serine). a class of proteolytic enzymes requiring the thiol group of a cysteine residue in the catalytic triad for their catalytic activity. a class of proteins that interact with GTPase in a GTP-dependent manner, which induces the downstream signaling pathway. an irreversible covalent modification of the N-terminal Gly residue with a 14-carbon myristate group, which is catalyzed by N-myristoyl transferases (NMTs) after the exposure of the N-terminal Gly residue in the conserved MGxxxS/T motif. The N-myristoylation of Gly contributes to protein–protein and protein–membrane interactions, which are involved in membrane trafficking, signal transduction, apoptosis, and protein secretion. a post-translational lipid modification that refers to a C15 (farnesyl) or C20 (geranylgeranyl) isoprenyl moiety attached to the C-terminal cysteine residue of the target protein by farnesyltransferase (FTase) or geranylgeranyltransferase type I (GGTase I), respectively. a complex macromolecular machine involved in the transfer of virulence proteins into host cells. a type of T4SS encoded by dot/icm genes and responsible for the injection of Legionella effectors into infected cells." @default.
• W3094256900 created "2020-10-29" @default.
• W3094256900 creator A5040062912 @default.
• W3094256900 creator A5043934036 @default.
• W3094256900 creator A5048839212 @default.
• W3094256900 creator A5061620214 @default.
• W3094256900 date "2021-03-01" @default.
• W3094256900 modified "2023-10-17" @default.
• W3094256900 title "Host Delipidation Mediated by Bacterial Effectors" @default.
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