Proximal protein tyrosine kinases in immunoreceptor signaling

Latour, Sylvain; Veillette, André

doi:10.1016/s0952-7915(00)00219-3

Cited by 176 publications

(159 citation statements)

References 61 publications

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“…Syk/ZAP70 family PTKs are functionally coupled to several immunoreceptors and critically contribute to the signaling and functional ability of Ag and Fc receptors on T, B, and NK lymphocytes, myeloid cells, and platelets (33)(34)(35). Syk and ZAP70 are highly homologous; nevertheless, they do not seem to fulfill redundant roles.…”

Section: Discussionmentioning

confidence: 99%

“…However, it cannot be ruled out that a low grade autophosphorylation of Syk may also play a role. Syk activation has been shown to involve several mechanisms, including a conformational change due to ITAM binding, autophosphorylation, and phosphorylation by other kinases (33)(34)(35). The relative importance of such mechanisms may be dictated by the modalities regulating Syk recruitment to different receptors.…”

Section: Discussionmentioning

confidence: 99%

“…The PTK-dependent activation of Syk by immunoreceptors may depend on autophosphorylation or be under the control of Src family kinases (33)(34)(35); no definitive information exists on the upstream events involved in Syk activation upon engagement of NKactivating receptors. To address the role of Src family kinases in CD69-triggered activation of Syk, we initially used the Src-selective pharmacological inhibitor PP2 (36).…”

Section: Cd69-triggered Activation Of Syk Is Mediated By Lckmentioning

confidence: 99%

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Src-Dependent Syk Activation Controls CD69-Mediated Signaling and Function on Human NK Cells

Pisegna

Zingoni

Pirozzi

et al. 2002

The Journal of Immunology

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CD69 C-type lectin receptor represents a functional triggering molecule on activated NK cells, capable of directing their natural killing function. The receptor-proximal signaling pathways activated by CD69 cross-linking and involved in CD69-mediated cytotoxic activity are still poorly understood. Here we show that CD69 engagement leads to the rapid and selective activation of the tyrosine kinase Syk, but not of the closely related member of the same family, ZAP70, in IL-2-activated human NK cells. Our results indicate the requirement for Src family kinases in the CD69-triggered activation of Syk and suggest a role for Lck in this event. We also demonstrate that Syk and Src family tyrosine kinases control the CD69-triggered tyrosine phosphorylation and activation of phospholipase Cγ2 and the Rho family-specific exchange factor Vav1 and are responsible for CD69-triggered cytotoxicity of activated NK cells. The same CD69-activated signaling pathways are also observed in an RBL transfectant clone, constitutively expressing the receptor. These data demonstrate for the first time that the CD69 receptor functionally couples to the activation of Src family tyrosine kinases, which, by inducing Syk activation, initiate downstream signaling pathways and regulate CD69-triggered functions on human NK cells.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Cd69-triggered Activation Of Syk Is Mediated By Lckmentioning

confidence: 99%

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Src-Dependent Syk Activation Controls CD69-Mediated Signaling and Function on Human NK Cells

Pisegna

Zingoni

Pirozzi

et al. 2002

The Journal of Immunology

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“…In particular, in breast cancer cells, upon cell-ECM adhesion or epidermal growth factor (EGF) stimulation, p140CAP activates CSK kinase 40 , which by phosphorylating the inhibitory tyrosine on the C-terminal domain of SRC, allows the closure of SRC in an inactive conformation 114 (Figure 4a). Therefore p140CAP represents a new potent regulator of the protooncogene SRC that is able to shift the balance between active or inactive SRC.…”

Section: The Cap Family In Cancer Biologymentioning

confidence: 99%

Integrin signalling adaptors: not only figurants in the cancer story

et al. 2010

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Current evidence highlights the ability of adaptor (or scaffold) proteins to create signalling platforms that drive cellular transformation upon integrin-dependent adhesion and growth factor receptor activation. The understanding of the biological effects regulated by these adaptors in tumours might be crucial for the identification of novel targets and the development of innovative therapeutic strategies for human cancer. In this review we will discuss the relevance of adaptor proteins in signalling originating from integrin-mediated cell-extracellular matrix (ECM) adhesion and growth factor stimulation within the context of cell transformation and tumour progression.Herein, we will specifically underline the contribution of p130CAS, NEDD9, CRK, and the IPP complex (ILK, PINCH and PARVIN) to cancer, along with the more recently identified p140CAP.

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“…Activation of the T-cell antigen receptor (TCR) results in the recruitment and activation of members of both the Src and Syk families of cytoplasmic tyrosine kinases (reviewed in Latour and Veillette, 2001). The subsequent phosphorylation of downstream targets by these kinases triggers a signalling cascade that ultimately results in the transcriptional upregulation of genes such as IL-2, a growth-promoting cytokine.…”

Section: Introductionmentioning

confidence: 99%