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#post-translational modifications

3 public questions tagged with this topic.

Which lipid-linked protein modification is not reversible?

Lipid modifications vary in stability and enzymatic reversibility enabling dynamic membrane association. Palmitoylation S-acylation via DHHC family palmitoyl acyltransferases forming thioester linkage can be removed by acyl protein thioesterases APT1, APT2 and ABHD17 family allowing cycles of membrane binding and cytosolic redistribution crucial for neuronal signaling proteins like PSD-95 and H-Ras. Prenylation thioether linkage is irreversible chemically stable requiring proteolysis for reversal; however protease cleavage of prenylated C-terminus does not regenerate unmodified cysteine. GPI a

Ref: Resh, Nat Chem Biol 2013, Reversibility of lipid modifications; Chamberlain & Shipston, Physiol Rev 2015.

A blot to confirm post-translational lipid modifications:

Post-translational lipid attachments including myristoylation, palmitoylation, prenylation, and glycosylphosphatidylinositol anchor addition influence membrane targeting, signal transduction, and protein stability. Standard immunodetection recognizes polypeptide backbone but does not confirm lipid adduct. Eastern blotting was introduced to address this gap by combining protein separation and transfer with detection specifically directed against lipid or carbohydrate moieties using chemical stains, lectins, or lipid-specific reagents. Southern and Northern techniques target nucleic acids, while

Ref: NCERT Biology Class XII Principles on Klenow fill-in labeling, Lehninger Chapter 9 DNA cloning techniques, and Molecular Cloning by Sambrook Chapter 10 documenting end-labeling of cohesive termini.