P. Rougerie and J. Delon, Rho GTPases: masters of T lymphocyte migration and activation, Immunol Lett, vol.142, pp.1-13, 2012.

J. Cherfils and M. Zeghouf, Regulation of small GTPases by GEFs, GAPs, and GDIs, Physiol Rev, vol.93, pp.269-309, 2013.

G. R. Hoffman, N. Nassar, and R. A. Cerione, Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI, Cell, vol.100, pp.345-56, 2000.

Y. Gernez, A. A. De-jesus, H. Alsaleem, C. Macaubas, A. Roy et al., Severe autoinflammation in 4 patients with C-terminal variants in cell division control protein 42 homolog (CDC42) successfully treated with IL-1b inhibition, J Allergy Clin Immunol, vol.144, pp.1122-1127, 2019.

M. T. Lam, S. Coppola, O. Krumbach, G. Prencipe, A. Insalaco et al., A novel disorder involving dyshematopoiesis, inflammation, and HLH due to aberrant CDC42 function, J Exp Med, vol.216, pp.2778-99, 2019.

L. Pfajfer, N. K. Mair, R. Jimenez-heredia, F. Genel, N. Gulez et al., Mutations affecting the actin regulator WD repeat-containing protein 1 lead to aberrant lymphoid immunity, J Allergy Clin Immunol, vol.142, pp.1589-604, 2018.

M. K. Akula, M. Shi, Z. Jiang, C. E. Foster, D. Miao et al., Control of the innate immune response by the mevalonate pathway, Nat Immunol, vol.17, pp.922-931, 2016.

Y. H. Park, G. Wood, D. L. Kastner, and J. J. Chae, Pyrin inflammasome activation and RhoA signaling in the autoinflammatory diseases FMF and HIDS, Nat Immunol, vol.17, pp.914-935, 2016.

M. K. Akula, M. X. Ibrahim, E. G. Ivarsson, O. M. Khan, I. T. Kumar et al., Protein prenylation restrains innate immunity by inhibiting Rac1 effector interactions, Nat Commun, vol.3975, 2019.

. References-e1, L. I. Salazar-fontana, V. Barr, L. E. Samelson, and B. E. Bierer, CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells, J Immunol, vol.171, pp.2225-2257, 2003.

S. Faure, L. I. Salazar-fontana, M. Semichon, V. L. Tybulewicz, G. Bismuth et al., ERM proteins regulate cytoskeleton relaxation promoting T cell-APC conjugation, Nat Immunol, vol.5, pp.272-281, 2004.

E. Bal, H. S. Park, Z. Belaid-choucair, H. Kayserili, M. Naville et al., Mutations in ACTRT1 and its enhancer RNA elements lead to aberrant activation of Hedgehog signaling in inherited and sporadic basal cell carcinomas, Nat Med, vol.23, pp.1226-1259, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02415844

P. Poullet, S. Carpentier, and E. Barillot, myProMS, a web server for management and validation of mass spectrometry-based proteomic data, Proteomics, vol.7, pp.2553-2559, 2007.

B. Valot, O. Langella, E. Nano, and M. Zivy, MassChroQ: a versatile tool for mass spectrometry quantification, Proteomics, vol.11, pp.3572-3579, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01481216

J. A. Vizcaino, A. Csordas, N. Del-toro, J. A. Dianes, J. Griss et al., update of the PRIDE database and its related tools, Nucleic Acids Res, vol.44, p.11033, 2016.

, or minus SEs of at least 3 independent experiments. The levels of significance were calculated by ANOVA or the Student t test: *P < .05

*. ***p-<-.001 and . ***p-<, , p.1