Proteolytic processing of the receptor‐type protein tyrosine phosphatase PTPBR7
The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post‐translational modifications imposed on th...
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| Published in | The FEBS journal Vol. 274; no. 1; pp. 96 - 108 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Publishing Ltd
01.01.2007
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1742-464X 1742-4658 |
| DOI | 10.1111/j.1742-4658.2006.05568.x |
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| Abstract | The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post‐translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP‐SL, PTPPBSγ42 and PTPPBSγ37, which have distinct N‐terminal segments and localize to different parts of the cell. All isoforms were found to be short‐lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N‐terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65‐kDa transmembrane PTPRR isoform. Unlike for some other receptor‐type PTPs, the proteolytically produced N‐terminal ectodomain does not remain associated with this PTPRR‐65. Shedding of PTPBR7‐derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. |
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| AbstractList | The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBSgamma42 and PTPPBSgamma37, which have distinct N-terminal segments and localize to different parts of the cell. All isoforms were found to be short-lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform. Unlike for some other receptor-type PTPs, the proteolytically produced N-terminal ectodomain does not remain associated with this PTPRR-65. Shedding of PTPBR7-derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post‐translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP‐SL, PTPPBSγ42 and PTPPBSγ37, which have distinct N‐terminal segments and localize to different parts of the cell. All isoforms were found to be short‐lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N‐terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65‐kDa transmembrane PTPRR isoform. Unlike for some other receptor‐type PTPs, the proteolytically produced N‐terminal ectodomain does not remain associated with this PTPRR‐65. Shedding of PTPBR7‐derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post‐translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP‐SL, PTPPBSγ42 and PTPPBSγ37, which have distinct N‐terminal segments and localize to different parts of the cell. All isoforms were found to be short‐lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N‐terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65‐kDa transmembrane PTPRR isoform. Unlike for some other receptor‐type PTPs, the proteolytically produced N‐terminal ectodomain does not remain associated with this PTPRR‐65. Shedding of PTPBR7‐derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBSgamma42 and PTPPBSgamma37, which have distinct N-terminal segments and localize to different parts of the cell. All isoforms were found to be short-lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform. Unlike for some other receptor-type PTPs, the proteolytically produced N-terminal ectodomain does not remain associated with this PTPRR-65. Shedding of PTPBR7-derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology.The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBSgamma42 and PTPPBSgamma37, which have distinct N-terminal segments and localize to different parts of the cell. All isoforms were found to be short-lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform. Unlike for some other receptor-type PTPs, the proteolytically produced N-terminal ectodomain does not remain associated with this PTPRR-65. Shedding of PTPBR7-derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBS gamma 42 and PTPPBS gamma 37, which have distinct N-terminal segments and localize to different parts of the cell. All isoforms were found to be short-lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform. Unlike for some other receptor-type PTPs, the proteolytically produced N-terminal ectodomain does not remain associated with this PTPRR-65. Shedding of PTPBR7-derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology. |
| Author | van de Vorstenbosch, Rinske Dilaver, Gönül Ríos, Pablo Fransen, Jack Hendriks, Wiljan Pulido, Rafael van Aerde, Karlijn Tárrega, Céline |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17147696$$D View this record in MEDLINE/PubMed |
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Alternative splicing produces transmembrane, cytosolic and truncated isoforms publication-title: Eur J Cell Biol |
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| Snippet | The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters,... The single‐copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters,... The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters,... |
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| SubjectTerms | Animals Brain - metabolism Fluorescent Antibody Technique Intracellular Signaling Peptides and Proteins - metabolism Mice Mice, Inbred C57BL Neurons Phosphorylation post‐translational modification Protein Isoforms - metabolism protein phosphorylation Protein Processing, Post-Translational protein stability Protein Tyrosine Phosphatases - metabolism Proteins Proteomics PTPRR Receptor-Like Protein Tyrosine Phosphatases, Class 7 Recombinant Fusion Proteins - metabolism Rodents Signal transduction |
| Title | Proteolytic processing of the receptor‐type protein tyrosine phosphatase PTPBR7 |
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