Primary sequence determinants responsible for site‐selective dephosphorylation of the PDGF β‐receptor by the receptor‐like protein tyrosine phosphatase DEP‐1

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Abstract
Site‐selective dephosphorylation of receptor tyrosine kinases contributes to receptor regulation. The receptor‐like protein tyrosine phosphatase DEP‐1 site‐selectively dephosphorylates the PDGF β‐receptor. DEP‐1 dephosphorylation of original and chimeric phospho‐peptides spanning the preferred pY1021 and the less preferred pY857 and pY562 sites was analyzed. Double substitutions of basic residues at −4 and +3 of pY857 and pY562 peptides improved affinity. Substitutions of single amino acids indicated preference for an acidic residue at position −1 and a preference against a basic residue at position +3. DEP‐1 site‐selective dephosphorylation of PDGF β‐receptor is thus determined by the primary sequence surrounding phosphorylation sites and involves interactions with residues spanning at least between positions −1 and +3.

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