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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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 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.[1]

References

  1. Proteolytic processing of the receptor-type protein tyrosine phosphatase PTPBR7. Dilaver, G., van de Vorstenbosch, R., Tárrega, C., Ríos, P., Pulido, R., van Aerde, K., Fransen, J., Hendriks, W. FEBS J. (2007) [Pubmed]
 
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