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- Title
Protein tyrosine phosphatase receptor type Z is inactivated by ligand-induced oligomerization
- Authors
Fukada, Masahide; Fujikawa, Akihiro; Chow, Jeremy P.H.; Ikematsu, Shinya; Sakuma, Sadatoshi; Noda, Masaharu
- Abstract
Abstract: 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.
- Subjects
TYROSINE; G proteins; MEMBRANE proteins; PHOSPHORYLATION
- Publication
FEBS Letters, 2006, Vol 580, Issue 17, p4051
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.06.041