Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1
2002 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 517, no 1-3, 27-31 p.Article in journal (Refereed) Published
Site-selective dephosphorylation of receptor tyrosine kinases contributes to receptor regulation. The receptor-like protein tyrosine phosphatase DEP-1 site-selectively dephosphorylates the PDGF beta-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 beta-receptor is thus determined by the primary sequence surrounding phosphorylation sites and involves interactions with residues spanning at least between positions -1 and +3.
Place, publisher, year, edition, pages
2002. Vol. 517, no 1-3, 27-31 p.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-90185DOI: 10.1016/S0014-5793(02)02570-XPubMedID: 12062403OAI: oai:DiVA.org:uu-90185DiVA: diva2:162450