Dephosphorylation

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Dephosphorylation

 

the splitting-off of a phosphoric acid group from a molecule of a compound containing phosphorus. Some unstable organic phosphorus compounds can undergo spontaneous dephosphorylation, but in living organisms dephosphorylation proceeds primarily with the participation of enzymes. Dephosphorylation brought about by kinases (creatine kinase, glucokinase, and so on) leads to the transfer of the phosphoric acid group to other compounds. Dephosphorylation that is catalyzed by phosphorylases (phosphoamidases) results in the formation of free phosphoric acid. The differentiation among the various types of fermentative dephosphorylation is to some extent arbitrary.

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ITIM in CD72 is then tyrosine-phosphorylated by BCR-associated kinases, such as Lyn, and recruits and activates SHP-1, which in turn inactivates BCR signaling by dephosphorylating various signaling molecules.
It acts as a negative regulator of PI3 K by dephosphorylating phosphatidylinositol 3,4,5 triphosphate, inactivating downstream effectors, notably Akt (Seront et al.
PKG also activates protein phosphatases, dephosphorylating molecular motor-associated proteins such as the 20-kDa myosin light chain (MLC) (Lincoln, 2007).
Endogenous phosphatases and dephosphorylating DNA under an acidic condition have been also identified in lenses [27, 28].
Similarly, reduced expression of signalling pathway components such as phosphatase and tensin homologue (PTEN) involved in negative regulation of PI3K signalling, by dephosphorylating PIP3 in this signal transduction pathway, may prevent the anti-tumour effects of the antibody.
49,65,66) In addition, CagA-deregulated SHP2 down-regulates the kinase activity of focal adhesion kinase (FAK) by dephosphorylating the activating phosphotyrosine residues (Tyr-369, -574, and -575), resulting in impaired focal adhesion turnover.