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Protein tyrosine phosphatase receptor type Z is inactivated by ligand‐induced oligomerization
Author(s) -
Fukada Masahide,
Fujikawa Akihiro,
Chow Jeremy P.H.,
Ikematsu Shinya,
Sakuma Sadatoshi,
Noda Masaharu
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.06.041
Subject(s) - protein tyrosine phosphatase , pleiotrophin , phosphatase , receptor tyrosine kinase , biochemistry , chemistry , phosphorylation , tyrosine , tyrosine kinase , extracellular , ligand (biochemistry) , microbiology and biotechnology , receptor , biology , growth factor
Receptor‐type protein tyrosine phosphatases (RPTPs) are considered to transduce extracellular signals across the membrane through changes in their PTP activity, however, our understanding of the regulatory mechanism is still limited. Here, we show that pleiotrophin (PTN), a natural ligand for protein tyrosine phosphatase receptor type Z (Ptprz) (also called PTPζ/RPTPβ), inactivates Ptprz through oligomerization and increases the tyrosine phosphorylation of substrates for Ptprz, G protein‐coupled receptor kinase‐interactor 1 (Git1) and membrane associated guanylate kinase, WW and PDZ domain containing 1 (Magi1). Oligomerization of Ptprz by an artificial dimerizer or polyclonal antibodies against its extracellular region also leads to inactivation, indicating that Ptprz is active in the monomeric form and inactivated by ligand‐induced oligomerization.