ArticleCellular signalling2008
Role of chimaerins, a group of Rac-specific GTPase activating proteins, in T-cell receptor signaling.
Article in Cellular signalling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- β2-Chimaerin Deficiency Favors Polyp Growth in the Colon of ApcMolecules (Basel, Switzerland) · 2025Article
- β2-Chimaerin, a GTPase-Activating Protein for Rac1, Is a Novel Regulator of Hepatic Insulin Signaling and Glucose Metabolism.Molecules (Basel, Switzerland) · 2024Article
- Identification of a truncated β1-chimaerin variant that inactivates nuclear Rac1.The Journal of biological chemistry · 2020Article
- A new role of the Rac-GAP β2-chimaerin in cell adhesion reveals opposite functions in breast cancer initiation and tumor progression.Oncotarget · 2016Article
- Diacylglycerol Kinases in T Cell Tolerance and Effector Function.Frontiers in cell and developmental biology · 2016Review
- Article
- Regulation of ras exchange factors and cellular localization of ras activation by lipid messengers in T cells.Frontiers in immunology · 2013Review
- Regulation of Lipid Signaling by Diacylglycerol Kinases during T Cell Development and Function.Frontiers in immunology · 2013Article
- Coordinated activation of the Rac-GAP β2-chimaerin by an atypical proline-rich domain and diacylglycerol.Nature communications · 2013Article
- Rac1 protein regulates glycogen phosphorylase activation and controls interleukin (IL)-2-dependent T cell proliferation.The Journal of biological chemistry · 2012Article
- Lipid signaling in T-cell development and function.Cold Spring Harbor perspectives in biology · 2010Review
- Article
- Biochemical characterization of hyperactive beta2-chimaerin mutants revealed an enhanced exposure of C1 and Rac-GAP domains.Biochemistry · 2009Article
- Localized diacylglycerol drives the polarization of the microtubule-organizing center in T cells.Nature immunology · 2009Article
- T cell receptor-dependent tyrosine phosphorylation of beta2-chimaerin modulates its Rac-GAP function in T cells.The Journal of biological chemistry · 2009Article
- Mechanistic analysis of the amplification and diversification events induced by Vav proteins in B-lymphocytes.The Journal of biological chemistry · 2008Article
- Identification of an autoinhibitory mechanism that restricts C1 domain-mediated activation of the Rac-GAP alpha2-chimaerin.The Journal of biological chemistry · 2008Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Chimaerins are GTPase-activating proteins that inactivate the GTP-hydrolase Rac1 in a diacylglycerol-dependent manner. To date, the study of chimaerins has been done mostly in neuronal cells. Here, we show that alpha2- and beta2-chimaerin are expressed at different levels in T-cells and that they participate in T-cell receptor signaling. In agreement with this, we have observed that alpha2- and beta2-chimaerins translocate to the T-cell/B-cell immune synapse and, using both gain- and loss-of-function approaches, demonstrated that their catalytic activity is important for the inhibition of the T-cell receptor- and Vav1-dependent stimulation of the transcriptional factor NF-AT. Mutagenesis-based approaches have revealed the molecular determinants that contribute to the biological program of chimaerins during T-cell responses. Unexpectedly, we have found that the translocation of chimaerins to the T-cell/B-cell immune synapse does not rely on the canonical binding of diacylglycerol to the C1 region of these GTPase-activating proteins. Taken together, these results identify chimaerins as candidates for the downmodulation of Rac1 in T-lymphocytes and, in addition, uncover a novel regulatory mechanism that mediates their activation in T-cells.
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