2008
DOI: 10.1016/j.bbamcr.2007.10.023
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Multimerisation of receptor-type protein tyrosine phosphatases PTPBR7 and PTP-SL attenuates enzymatic activity

Abstract: Dimerisation of receptor-type protein tyrosine phosphatases (RPTPs) represents an appealing mechanism to regulate their enzymatic activity. Studies thus far mostly concern the dimerisation behaviour of RPTPs possessing two tandemly oriented catalytic PTP domains. Mouse gene Ptprr encodes four different protein isoforms (i.e. PTPBR7, PTP-SL and PTPPBSgamma-42/37) that contain a single PTP domain. Using selective membrane permeabilisation we here demonstrate that PTP-SL, like PTPBR7, is a single membrane-spannin… Show more

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Cited by 10 publications
(23 citation statements)
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“…As we show below, the pan-PTP inhibitor Na 2 VO 3 (19,20), which should inhibit PTP-SL (15), does not block FSH-stimulated ERK phosphorylation. PTP-SL has a molecular weight of ϳ55 kDa, not 100 kDa (21). A second antibody directed against PTPBR7, another phosphatase sharing protein sequence homology with PTP-SL except for a 127-amino acid insertion in the N terminus (14), does not detect a signal on Western blotting analyses of GC extracts at 100 kDa (10).…”
mentioning
confidence: 99%
“…As we show below, the pan-PTP inhibitor Na 2 VO 3 (19,20), which should inhibit PTP-SL (15), does not block FSH-stimulated ERK phosphorylation. PTP-SL has a molecular weight of ϳ55 kDa, not 100 kDa (21). A second antibody directed against PTPBR7, another phosphatase sharing protein sequence homology with PTP-SL except for a 127-amino acid insertion in the N terminus (14), does not detect a signal on Western blotting analyses of GC extracts at 100 kDa (10).…”
mentioning
confidence: 99%
“…Depending on the translational start site choice, the other isoforms produce either PTP-SL-like vesicle-associated versions or, more likely, cytosolic proteins that resemble murine PTPPBSγ. Intriguingly, the mouse transmembrane PTPRR isoforms form multimeric complexes and their relative PTP activity is significantly lower than that of the cytosolic PTPPBSγ type (Noordman et al, 2008). This predicts regulatory potential for any biomolecule that would bind to the PTPBR7 and/or PTP-SL parts that are N-terminal of the transmembrane segment.…”
Section: Localisationmentioning
confidence: 99%
“…No detailed studies on the subcellular localization of human PTPRR protein isoforms have been performed and, again, only inference from mouse and rat data (Shiozuka et al, 1995;Ogata et al, 1999;Van Den Maagdenberg et al, 1999;Dilaver et al, 2003;Noordman et al, 2006;Noordman et al, 2008;Hendriks et al, 2009) remains. Based on this, it seems reasonable to postulate that isoform #1 will display a PTPBR7-like cell surface expression and that isoform #3 may reside on the trans-Golgi network and multivesicular bodies or sorting endosomes, like mouse PTP-SL does.…”
Section: Localisationmentioning
confidence: 99%
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