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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Curr Opin Microbiol. 2010 Jan 12;13(1):34–40. doi: 10.1016/j.mib.2009.12.004

Figure 3. Posttranslational modifications altering protein phosphorylation state.

Figure 3

A. YopH dephosphorylates the tyrosine residue of multiple proteins at the cellular membrane, resulting in loss of focal adhesion complexes and alteration of the actin cytoskeleton blocking phagocytosis of extracellular bacteria. B. SopB alters multiple signaling cascades through the dephosphorylation of inositol moieties at multiple membranes in the host cell. C. YpkA inactivates Gαq by phosphorylating the diphosphate loop, blocking nucleotide binding through steric hindrance leading to a loss of downstream PLC-β and Rho GTPase activation. D. OspF mediates the irreversible β-elimination of a phosphothreonine residue on MAPK to dehydrobutyrine with the release of inorganic phosphate, blocking MAPK signaling.