Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains.

Uchida, Tsuyoshi; Matozaki, Takashi; Noguchi, Tetsuya; Yamao, Takuji; Horita, K; Suzuki, Toshiya; Fujioka, Yohsuke; Sakamoto, Choitsu; Kasuga, Masato

doi:10.1016/s0021-9258(17)32704-7

Cited by 124 publications

(15 citation statements)

References 49 publications

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“…An understanding of the consequences of this phosphorylation on LAR-PTP activity will require the identification and mutation of the TrkAinduced tyrosine phosphorylation sites. There is precedent for regulation of PTPs by tyrosine phosphorylation: the nonreceptor phosphatase, PTP1C, is phosphorylated on tyrosine in response to insulin receptor activation, and this correlates with an increase in its activity (Uchida et al, 1994); RPTPa is phosphorylated constitutively on tyrosine (den Hertog et al, 1994;Suet al, 1994), and in vitro experiments suggest that tyrosine phosphorylation reduces the activity of this phosphatase (den Hertog et al, 1994). Therefore, TrkA-induced phosphorylation of LAR-PTPs provides a potential mechanism for regulating their activities.…”

Section: Discussionmentioning

confidence: 99%

Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex.

Kypta

Reichardt

1996

The Journal of Cell Biology

236

158

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Abstract. Cadherins are calcium-dependent cell adhesion molecules that play fundamental roles in embryonic development, tissue morphogenesis, and cancer. A prerequisite for their function is association with the actin cytoskeleton via the catenins. Tyrosine phosphorylation of 13-catenin, which correlates with a reduction in cadherin-dependent cell adhesion, may provide cells with a mechanism to regulate cadherin activity. Here we report that ~3-catenin immune precipitates from PC12 cells contain tyrosine phosphatase activity which dephosphorylates 13-catenin in vitro. In addition, we show that a member of the leukocyte antigen-related protein (LAR)-related transmembrane tyrosine phosphatase family (LAR-PTP) associates with the cadherin-catenin complex. This association requires the amino-terminal domain of 13-catenin but does not require the armadillo repeats, which mediate association with cadherins. The interaction also is detected in PC9 cells, which lack a-catenin. Thus, the association is not mediated by a-catenin or by cadherins. Interestingly, LAR-PTPs are phosphorylated on tyrosine in a TrkAdependent manner, and their association with the cadherin--catenin complex is reduced in cells treated with NGF. We propose that changes in tyrosine phosphorylation of ~3-catenin mediated by TrkA and LAR-PTPs control cadherin adhesive function during processes such as neurite outgrowth.

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Section: Discussionmentioning

confidence: 99%

Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex.

Kypta

Reichardt

1996

The Journal of Cell Biology

236

158

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“…Here, phosphotyrosines on the activated RTK bind SHP1 via its SH2 domain, which allosterically activates the phosphatase. Phosphorylation of SHP1 by the RTK then locks it into the active state, irrespective of binding to the RTK (Frank et al, 2004;Uchida et al, 1994). In spite of the high similarity with the excitable media network structure discussed above, the spatial outcome is exactly the opposite, as it focuses global activation into local hot spots (Figure 1C).…”

Section: Signaling Across a Dynamic Barrier: The Lateral Dimensionmentioning

confidence: 94%

Signaling from the Living Plasma Membrane

Grecco

Schmick

Bastiaens

2011

Cell

226

188

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Our understanding of the plasma membrane, once viewed simply as a static barrier, has been revolutionized to encompass a complex, dynamic organelle that integrates the cell with its extracellular environment. Here, we discuss how bidirectional signaling across the plasma membrane is achieved by striking a delicate balance between restriction and propagation of information over different scales of time and space and how underlying dynamic mechanisms give rise to rich, context-dependent signaling responses. In this Review, we show how computer simulations can generate counterintuitive predictions about the spatial organization of these complex processes.

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“…Another potential mode of regulation is the phosphorylation of SHP1 at Tyr-538 (Tyr-536 in mouse SHP1) upon various extracellular stimuli (276)(277), and also at Tyr-566 (Tyr-564 in mouse SHP1) in the Lckoverexpressing thymoma cell line LSTRA and in T cells (278). In vitro, Lck readily phosphorylates both these sites (our unpublished observation).…”

Section: Shp1 -A Negative Regulator Of Signalingmentioning

confidence: 99%