Molecular cloning of a novel protein‐tyrosine phosphatase SH‐PTP3 with sequence similarity to the <i>src</i>‐homology region 2

Adachi, Masaaki; Sekiya, Masuo; Miyachi, T; Matsuno, Kuniharu; Hinoda, Yuji; Imai, Kohzoh; Yachi, Akira

doi:10.1016/0014-5793(92)81500-l

Cited by 90 publications

(51 citation statements)

References 26 publications

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“…SHP-2, previously called SH-PTP2, PTP1D, SH-PTP3, and Syp, was identified independently by several groups as a cytosolic SH2 domain containing protein tyrosine phosphatase [4][5][6][7][8]. It is ubiquitously expressed in various tissues and cell types.…”

Section: Signaling Mechanismsmentioning

confidence: 99%

“…However, studies regarding PTPs are lagging behind. SHP-2, a Src homology 2 (SH2) domain containing nontransmembrane PTP, has been demonstrated to be involved in a variety of cytokine and growth factor initiated signal transduction processes [4][5][6][7][8]. Increasing evidence has indicated that this phosphatase plays an important role in diverse signaling pathways to regulate cellular biological processes.…”

Section: Introductionmentioning

confidence: 99%

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The SHP-2 tyrosine phosphatase: Signaling mechanisms and biological functions

2000

Cell Res

141

102

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Cellular biological activities are tightly controlled by intracellular signaling processes initiated by extracellular signals. Protein tyrosine phosphatases, which remove phosphate groups from tyrosine phosphorylated signaling molecules, play equally important tyrosine roles as protein kinases in signal transduction. SHP-2, a cytoplasmic SH2 domain containing protein tyrosine phosphatase, is involved in the signaling pathways of a variety of growth factors and cytokines. Recent studies have clearly demonstrated that this phosphatase plays an important role in transducing signal relay from the cell surface to the nucleus, and is a critical intracellular regulator in mediating cell proliferation and differentiation.

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Section: Signaling Mechanismsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The SHP-2 tyrosine phosphatase: Signaling mechanisms and biological functions

2000

Cell Res

141

102

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“…Another prominent one is the Akt pathway that seems to be important for the NF-kB activation (Sizemore et al, 1999;Ozes et al, 1999). In addition to Akt, SHP-2, a cytoplasmic tyrosine phosphatase containing SH2 domain (Freeman et al, 1992;Adachi et al, 1992), appears to modulate the NF-kB pathway (You et al, 2001). Although both the MEK1 -MAPK and the Akt-NF-kB pathways are critical for IL-1 and TNFa signaling, how they are activated remains to be explored.…”

mentioning

confidence: 99%

A role for SHPS-1/SIRPα1 in IL-1β- and TNFα-dependent signaling

et al. 2002

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We investigated the role of SHPS-1/SIRPa1 in IL-1b-and TNFa-dependent signaling that leads to the activation of Erk 1/2 and Akt. Treatment of Balb3T3 cells with IL-1b or TNFa activated tyrosine phosphorylation of SHPS-1, its association with SHP-2 and the phosphorylation of Erk 1/2 and Akt. PP1, a specific inhibitor for the Src family protein tyrosine kinases, strongly inhibited tyrosine phosphorylation of SHPS-1 and complex formation of SHPS-1 with SHP-2 by IL1b. In addition, PP1 substantially inhibited the IL-2b-and TNFa-dependent activation of Erk 1/2 and Akt. Exogenous expression of either SHPS-1 mutants that lack SHP-2 binding function or a dominant negative mutant of SHP-2 markedly inhibited the activation of Erk 1/2 and Akt by IL-1b, whereas wild type SHPS-1 did not. Moreover, IL-1b-stimulation induced association of SHPS-1 with IL-1RAcP, a second subunit of IL-1 receptor, whereas expression of SHPS-1 mutant that lack SHP-2 binding function clearly blocked the association and tyrosine phosphorylation of endogenous SHPS-1. Taken together, our results strongly suggest that activation of Erk 1/2 and Akt by proinflammatory cytokines requires tyrosine phosphorylation of SHPS-1 and subsequent association of SHPS-1 with SHP-2.

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“…SHPTP1 appears to function primarily as a negative regulator of multiple hematopoietic cytokine and growth factor signaling pathways, as vividly illustrated by the motheaten mouse phenotype, which results from mutations in the SHPTP1 gene (62,71). The second mammalian SHPTP, SHPTP2 (17), also referred to as Syp (15), PTP-1D (76), PTP-2C (82), and SH-PTP3 (1), is ubiquitously expressed. Like SHPTP1, SHPTP2 contains two SH2 domains, a functional PTP domain, and a C-terminal hydrophilic domain containing tyrosyl phosphorylation sites (4).…”

mentioning

confidence: 99%

Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression

Bennett

Hausdorff

O’Reilly

et al. 1996

Molecular and Cellular Biology

233

194

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Using transient overexpression and microinjection approaches, we examined SHPTP2's function in growth factor signaling. Overexpression of catalytically inactive SHPTP2 (PTP2CS) but not catalytically inactive SHPTP1, inhibited mitogen-activated protein (MAP) kinase activation and Elk-1 transactivation following epidermal growth factor (EGF) stimulation of 293 cells. An SHPTP2 mutant with both C-terminal tyrosyl phosphorylation sites converted to phenylalanine (PTP2YF) was also without effect; moreover, PTP2YF rescued PTP2CS-induced inhibition of EGF-induced Elk-1 transactivation. PTP2CS did not inhibit transactivation by activated Ras, suggesting that SHPTP2 acts upstream of or parallel to Ras. Neither PTP2CS nor PTP2YF inhibited platelet-derived growth factor (PDGF)-induced Elk-1 transactivation. Thus, protein-tyrosine phosphatase activity, but not tyrosyl phosphorylation of SHPTP2, is required for the immediate-early responses to EGF but not to PDGF. To determine whether SHPTP2 is required later in the cell cycle, we assessed S-phase entry in NIH 3T3 cells microinjected with anti-SHPTP2 antibodies or with a glutathione S-transferase (GST) fusion protein encoding both SH2 domains (GST-SH2). Microinjection of anti-SHPTP2 antibodies prior to stimulation inhibited EGF-but not PDGF-or serum-induced S-phase entry. Anti-SHPTP2 antibodies or GST-SH2 fusion protein could inhibit EGF-induced S-phase entry for up to 8 h after EGF addition. Although MAP kinase activation was detected shortly after EGF stimulation, no MAP kinase activation was detected around the restriction point. Therefore, SHPTP2 is absolutely required for immediateearly and late events induced by some, but not all, growth factors, and the immediate-early and late signal transduction pathways regulated by SHPTP2 are distinguishable.

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Molecular cloning of a novel protein‐tyrosine phosphatase SH‐PTP3 with sequence similarity to the src‐homology region 2

Cited by 90 publications

References 26 publications

The SHP-2 tyrosine phosphatase: Signaling mechanisms and biological functions

The SHP-2 tyrosine phosphatase: Signaling mechanisms and biological functions

A role for SHPS-1/SIRPα1 in IL-1β- and TNFα-dependent signaling

Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression

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