2003
DOI: 10.1074/jbc.m210028200
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The Role of C-terminal Tyrosine Phosphorylation in the Regulation of SHP-1 Explored via Expressed Protein Ligation

Abstract: The protein-tyrosine phosphatase SHP-1 plays a variety of roles in the "negative" regulation of cell signaling. The molecular basis for the regulation of SHP-1 is incompletely understood. Whereas SHP-1 has previously been shown to be phosphorylated on two tail tyrosine residues (Tyr 536 and Tyr 564 ) by several protein-tyrosine kinases, the effects of these phosphorylation events have been difficult to address because of the intrinsic instability of the linkages within a protein-tyrosine phosphatase. Using exp… Show more

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Cited by 133 publications
(126 citation statements)
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“…Consistent with this notion, our results suggest that the engagement of SHP-1 by the NH 2 -terminal ITAM tyrosine of Fc␥RIIa leads to the activation of SHP-1. Other studies have reported a secondary mechanism of SHP-1 activation involving phosphorylation of SHP-1 on its COOH-terminal located tyrosine residues (29). In our experiments, although tyrosine phosphorylation of SHP-1 was detectable after Fc␥RIIa clustering (Fig.…”
Section: Discussionsupporting
confidence: 42%
See 1 more Smart Citation
“…Consistent with this notion, our results suggest that the engagement of SHP-1 by the NH 2 -terminal ITAM tyrosine of Fc␥RIIa leads to the activation of SHP-1. Other studies have reported a secondary mechanism of SHP-1 activation involving phosphorylation of SHP-1 on its COOH-terminal located tyrosine residues (29). In our experiments, although tyrosine phosphorylation of SHP-1 was detectable after Fc␥RIIa clustering (Fig.…”
Section: Discussionsupporting
confidence: 42%
“…Deletion of the NH 2 -terminal SH2 domain, or engagement of the SH2 domains with cognate phosphopeptides has been shown to activate the phosphatase. Enzyme activity of SHP-1 is further enhanced by phosphorylation of tyrosines (Tyr 536 and Tyr 564 ) in the COOH-terminal region (29). The significance of the regulatory role of SHP-1 in the hematopoetic system is best exemplified in mice homozygous for motheaten (me/me) or motheaten viable (mev/mev) mutations (30 -32).…”
mentioning
confidence: 99%
“…Here, we observed that addition of TSLP increased the phosphorylation of Y536 in SHP-1 ( Fig. 6F and Table I), which increases the phosphatase activity of SHP-1 (77,78). Ptpn18, also designated as fetal liver phosphatase 1, is not a well-studied phosphatase and consists of a protein tyrosine phosphatase domain followed by a carboxyl-terminal domain of 160 amino acids.…”
Section: Tslp Signaling Networkmentioning
confidence: 55%
“…4A, the phosphatase activity of SHP-1 was strongly regulated by the N-SH2 domain and the PTP catalytic domain, such as Asp61 (in N-SH2) and Lys362 (in catalytic PTP; refs. 21,22,25,28). As SC-60 did not alter the phospho-status of SHP-1 to activate phosphatase activity, we further validated whether SC-60 increases SHP-1 activity by interfering with intramolecular inhibition.…”
Section: Sc-60 Relieves Autoinhibited Shp-1 By Interfering With the Imentioning
confidence: 63%