2026-04-27T19:47:45Zhttps://uvadoc.uva.es/oai/request

oai:uvadoc.uva.es:10324/98262021-06-23T09:49:21Zcom_10324_1133com_10324_931com_10324_894col_10324_1209

Fuente García, Miguel Ángel de la Sasahara, Yoji Calamito, Marco Antón, Inés María Elkhal, Abdallah Gallego, María Dolores Suresh, Koduro Siminovitch, Katherine Ochs, Hans D. Anderson, Kenneth C. Rosen, Fred S. Geha, Raif S. Ramesh, Narayanaswamy Wiskott Aldrich, Síndrome protéico Producción Científica Wiskott–Aldrich syndrome protein (WASP) is in a complex with WASP-interacting protein (WIP). WASP levels, but not mRNA levels, were severely diminished in T cells from WIP / mice and were increased by introduction of WIP in these cells. The WASP binding domain of WIP was shown to protect WASP from degradation by calpain in vitro. Treatment with the proteasome inhibitors MG132 and bortezomib increased WASP levels in T cells from WIP / mice and in T and B lymphocytes from two WAS patients with missense mutations (R86H and T45M) that disrupt WIP binding. The calpain inhibitor calpeptin increased WASP levels in activated T and B cells from the WASP patients, but not in primary T cells from the patients or from WIP / mice. Despite its ability to increase WASP levels proteasome inhibition did not correct the impaired IL-2 gene expression and low F-actin content in T cells from the R86H WAS patient. These results demonstrate that WIP stabilizes WASP and suggest that it may also be important for its function 2015-03-23 2015-03-23 2007 info:eu-repo/semantics/article Proceedings of the National Academy of Sciences U S A. 2007 Jan 16;104(3):926-31 0027-8424 http://uvadoc.uva.es/handle/10324/9826 10.1073/pnas.0610275104 926 3 931 Proceedings of the National Academy of Sciences 104 eng https://www.pnas.org/content/104/3/926 info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/4.0/ Attribution-NonCommercial-NoDerivatives 4.0 International National Academy of Sciences