TAILIEUCHUNG - Báo cáo khoa học: Proteolytic processing of the receptor-type protein tyrosine phosphatase PTPBR7

The single-copy mouse genePtprrgives 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, PTPPBSc42 and PTPPBSc37, which have distinct N-terminal segments and localize to dif-ferent parts of the cell. | ễFEBS Journal Proteolytic processing of the receptor-type protein tyrosine phosphatase PTPBR7 Gonul Dilaver1 Rinske van de Vorstenbosch1 Celine Tarrega2 Pablo Rios2 Rafael Pulido2 Karlijn van Aerde3 Jack Fransen1 and Wiljan Hendriks1 1 Department of Cell Biology Nijmegen Centre for Molecular Life Sciences Radboud University Nijmegen MedicalCentre the Netherlands 2 Centro de Investigacion Príncipe Felipe Valencia Spain 3 Centre for Neurogenomics and Cognitive Research Vrije Universiteit Amsterdam the Netherlands Keywords post-translationalmodification protein phosphorylation protein stability PTPRR signal transduction Correspondence W. Hendriks 283 Cell Biology Nijmegen Centre for Molecular Life Sciences Radboud University Nijmegen Medical Centre Geert Grooteplein 28 6525 GA Nijmegen the Netherlands Fax 31 24 3615317 Tel 31 24 3614329 E-mail Received 25 September 2006 revised 26 October 2006 accepted 2 November 2006 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 PTPPBSc42 and PTPPBSc37 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. doi Protein tyrosine .

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