2011
DOI: 10.1074/jbc.m110.157420
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Identification of New Substrates of the Protein-tyrosine Phosphatase PTP1B by Bayesian Integration of Proteome Evidence

Abstract: There is growing evidence that tyrosine phosphatases display an intrinsic enzymatic preference for the sequence context flanking the target phosphotyrosines. On the other hand, substrate selection in vivo is decisively guided by the enzyme-substrate connectivity in the protein interaction network. We describe here a system wide strategy to infer physiological substrates of protein-tyrosine phosphatases. Here we integrate, by a Bayesian model, proteome wide evidence about in vitro substrate preference, as deter… Show more

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Cited by 45 publications
(61 citation statements)
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“…PTP1B has been reported to reduce the phosphorylation of multiple EGFR signaling pathway components, including PLC-γ1, GAB1, SHP2, SHP, and EGFR itself (45). Although the involvement of other EGFR phosphatases (26) cannot be discounted, our study suggests that PTP1B is the primary EGFR phosphatase causally involved in PRL-3-driven EGFR hyperphosphorylation.…”
Section: Discussionmentioning
confidence: 72%
“…PTP1B has been reported to reduce the phosphorylation of multiple EGFR signaling pathway components, including PLC-γ1, GAB1, SHP2, SHP, and EGFR itself (45). Although the involvement of other EGFR phosphatases (26) cannot be discounted, our study suggests that PTP1B is the primary EGFR phosphatase causally involved in PRL-3-driven EGFR hyperphosphorylation.…”
Section: Discussionmentioning
confidence: 72%
“…Placing phosphatases in such an interaction web would help to infer the function of poorly characterized phosphatases and to identify potential substrates [12][13][14]. In order to offer a proteome-wide perspective of the phosphatase interactome, we have embarked on an extensive text-mining-assisted literature curation effort to extend phosphatase interaction information that was not yet covered by protein-protein interaction (PPI) databases.…”
Section: Interaction Tabmentioning
confidence: 99%
“…PTP1B (50). The model was highly effective in predicting actual PTP1B substrates, such as EGFR, but in addition, it predicted K8 as a very high ranking substrate with a score near that of EGFR (0.897 for K8 versus 0.926 for EGFR) (50).…”
Section: Discussionmentioning
confidence: 99%
“…The model was highly effective in predicting actual PTP1B substrates, such as EGFR, but in addition, it predicted K8 as a very high ranking substrate with a score near that of EGFR (0.897 for K8 versus 0.926 for EGFR) (50). Our present findings demonstrate that PTP1B is a bona fide K8 phosphatase and raise the possibility that PTP1B may be an important regulator of K8 function under various types of epithelial cell stress, including in the liver, which is a major site of PTP1B action (51).…”
Section: Discussionmentioning
confidence: 99%