Identification of novel splicing variants of protein tyrosine phosphatase receptor type Z

Akihiro Fujikawa, Jeremy Pak Hong Chow, Masahito Matsumoto, Ryoko Suzuki, Kazuya Kuboyama, Naoki Yamamoto, Masaharu Noda

研究成果: ジャーナルへの寄稿学術論文査読

10 被引用数 (Scopus)


Protein tyrosine phosphatase receptor type Z (PTPRZ, also known as PTP or RPTPβ) is preferentially expressed in the central nervous system (CNS). PTPRZ plays important roles during development and adulthood in CNS myelination, learning and memory. Three splicing isoforms for PTPRZ have been identified to date: two receptor type isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S. We herein identified novel PTPRZ receptor sub-isoforms without a seven-amino acid sequence encoded by exon 16. This sequence forms a part of the helix-turn-helix segment called the wedge structure, which is located at the Nterminal region in the membrane-proximal protein tyrosine phosphatase domain. In contrast to conventional receptor isoforms with uniform expression, the deleted isoforms were expressed in the brain, but not in the retina, indicating the tissue-specific splicing of exon 16. Biochemical analyses of PTPRZ intracellular regions revealed differences in the characteristics of the deleted form, namely, stronger binding activity to postsynaptic density protein 95 (PSD95) and greater enrichment in the postsynaptic density fraction than the full-length form. Furthermore, the exon 16-deleted form exhibited higher catalytic efficiency in vitro. These results suggest that sub-isoforms of PTPRZ have different functions because of variations in the wedge structure.

ジャーナルJournal of Biochemistry
出版ステータス出版済み - 01-11-2017

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学


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