A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain

Hendriks, W; Schepens, J; Brugman, C; Zeeuwen, P; Wieringa, B

doi:10.1042/bj3050499

Cited by 52Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingCytokine Signaling Pathways and Interactions

A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain

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Hendriks, W, Schepens, J, Brugman, C, Zeeuwen, P, Wieringa, B·1995·Biochemical Journal

DOI 10.1042/bj3050499PMC PMC1136390

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Abstract

Protein tyrosine phosphatases (PTPases) are important regulatory proteins that, together with protein tyrosine kinases, determine the phosphotyrosine levels in cell signalling proteins. By PCR amplification of mouse brain cDNA fragments encoding the catalytic domains of these enzymes, we identified three novel members of the PTPase gene family. Northern-blot analysis showed that two of these novel clones represent brain-specific PTPases, whereas the third originates from a large-sized mRNA that is more ubiquitously expressed. A full-length cDNA encoding one of the brain-specific PTPases, PTP-SL, was isolated. Sequence analysis revealed a transmembrane PTPase containing a single catalytic phosphatase domain that has 45% homology to a rat cytoplasmic brain-specific PTPase named STEP. This suggests a role for PTP-SL in cell-cell signalling processes in the brain.

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KIM-PTPs HePTP, STEP, and PTPSL possess an N-terminal unstructured extension that includes the KIM, followed by their C-terminal phosphatase domain.
“Furthermore, the KIM-PTPs [Fig.1(B), center; hematopoietic tyrosine phosphatase, HePTP, immune system specific; 25 striatum-enriched phosphatase, STEP, brain specific; 26 STEP-like PTP, PTPSL, brain specific 27 ) also possess an N-terminal unstructured extension, which includes the KIM, followed by their C-terminal phosphatase domain (PTP).”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [27]

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Self-citation

Authors: Hendriks, W., Schepens, J., Brugman, C., Zeeuwen, P., & Wieringa, B.
Affiliations: Radboud University Nijmegen (NL)
ORCID: Hendriks, W
Zeeuwen, P
Wieringa, B
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1995-01-15
Volume: 305
Issue: 2
Pages: 499-504
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3050499
PMC: PMC1136390
OpenAlex: W2396708728
Cited by: 52
References: 51
Citations by year: 2026: 1 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 1
FWCI: 1.36
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Radboud Repository (Radboud University) (submittedVersion)
Radboud Repository (Radboud University) (submittedVersion, other-oa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords: receptor-type protein tyrosine phosphatase, STEP, cDNA cloning, mouse brain
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Brain, Cloning, Molecular, Glutathione Transferase, Molecular Sequence Data, Nerve Tissue Proteins, Receptors, Cell Surface, Recombinant Fusion Proteins, Protein Biosynthesis, Blotting, Northern, Polymerase Chain Reaction, Protein Tyrosine Phosphatases, Sequence Homology, Amino Acid, Alternative Splicing, Sequence Analysis, DNA, DNA, Complementary, Intracellular Signaling Peptides and Proteins, Mice, Receptor-Like Protein Tyrosine Phosphatases, Class 7

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A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain

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