Multivalent lipid targeting by the calcium-independent C2A domain of synaptotagmin-like protein 4/granuphilin was written by Alnaas, Aml A.;Watson-Siriboe, Abena;Tran, Sherleen;Negussie, Mikias;Henderson, Jack A.;Osterberg, J. Ryan;Chon, Nara L.;Harrott, Beckston M.;Oviedo, Julianna;Lyakhova, Tatyana;Michel, Cole;Reisdorph, Nichole;Reisdorph, Richard;Shearn, Colin T.;Lin, Hai;Knight, Jefferson D.. And the article was included in Journal of Biological Chemistry in 2021.Formula: C39H76NO8P The following contents are mentioned in the article:
Synaptotagmin-like protein 4 (Slp-4), also known as granuphilin, is a Rab effector responsible for docking secretory vesicles to the plasma membrane before exocytosis. Slp-4 binds vesicular Rab proteins via an N-terminal Slp homol. domain, interacts with plasma membrane SNARE complex proteins via a central linker region, and contains tandem C-terminal C2 domains (C2A and C2B) with affinity for phosphatidylinositol-(4,5)-bisphosphate (PIP2). The Slp-4 C2A domain binds with low nanomolar apparent affinity to PIP2 in lipid vesicles that also contain background anionic lipids such as phosphatidylserine but much weaker when either the background anionic lipids or PIP2 is removed. Through computational and exptl. approaches, we show that this high-affinity membrane binding arises from concerted interaction at multiple sites on the C2A domain. In addition to a conserved PIP2-selective lysine cluster, a larger cationic surface surrounding the cluster contributes substantially to the affinity for physiol. relevant lipid compositions Although the K398A mutation in the lysine cluster blocks PIP2 binding, this mutated protein domain retains the ability to bind physiol. membranes in both a liposome-binding assay and MIN6 cells. Mol. dynamics simulations indicate several conformationally flexible loops that contribute to the nonspecific cationic surface. We also identify and characterize a covalently modified variant that arises through reactivity of the PIP2-binding lysine cluster with endogenous bacterial compounds and binds weakly to membranes. Overall, multivalent lipid binding by the Slp-4 C2A domain provides selective recognition and high-affinity docking of large dense core secretory vesicles to the plasma membrane. This study involved multiple reactions and reactants, such as (2R,9Z)-1-(((2-Aminoethoxy)(hydroxy)phosphoryl)oxy)-3-(palmitoyloxy)propan-2-yl oleate (cas: 26662-94-2Formula: C39H76NO8P).
(2R,9Z)-1-(((2-Aminoethoxy)(hydroxy)phosphoryl)oxy)-3-(palmitoyloxy)propan-2-yl oleate (cas: 26662-94-2) belongs to esters. Esters perform as high-grade solvents for a broad array of plastics, plasticizers, resins, and lacquers, and are one of the largest classes of synthetic lubricants on the commercial market. Polyesters are important plastics, with monomers linked by ester moieties. Esterification is the general name for a chemical reaction in which two reactants (typically an alcohol and an acid) form an ester as the reaction product. Esters are common in organic chemistry and biological materials.Formula: C39H76NO8P
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