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

Abstract:

:Protein tyrosine phosphatase receptor type Z (PTPRZ, also known as PTPζ 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 N-terminal 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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Fujikawa A,Chow JPH,Matsumoto M,Suzuki R,Kuboyama K,Yamamoto N,Noda M

doi

10.1093/jb/mvx042

subject

Has Abstract

pub_date

2017-11-01 00:00:00

pages

381-390

issue

5

eissn

0021-924X

issn

1756-2651

pii

3871390

journal_volume

162

pub_type

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