Allosteric activation of MALT1 by its ubiquitin-binding Ig3 domain

Autor: C. Mpamhanga, Justyna Iwaszkiewicz, Frederick W. Muskett, P.J. Coombs, Ming Zhang, B. Saxty, Mai Perroud, R. H. Cowan, Margot Thome, Gareth Hall, R. Baravalle, Rebekka Schairer, L.R. Hale, Carr, Chantal Décaillet

Publikováno v: Proc Natl Acad Sci U S A

The catalytic activity of the protease MALT1 is required for adaptive immune responses and regulatory T (Treg)-cell development, while dysregulated MALT1 activity can lead to lymphoma. MALT1 activation requires its monoubiquitination on lysine 644 (K

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16f36f1c44b408f49607cb06fd5beea7
https://europepmc.org/articles/PMC7022147/

Malt1-dependent RelB cleavage promotes canonical NF-κB activation in lymphocytes and lymphoma cell lines

Autor: Georg Lenz, Christiane Pelzer, Montserrat Guzzardi, Chantal Décaillet, Bernd Dörken, Margot Thome, Stephan Hailfinger, Maike Jaworski, Peter Lenz, Jean-Enno Charton, Hendrik Nogai, Michael Grau, Katrin Cabalzar

Publikováno v: Proceedings of the National Academy of Sciences. 108:14596-14601

The protease activity of the paracaspase Malt1 contributes to antigen receptor-mediated lymphocyte activation and lymphomagenesis. Malt1 activity is required for optimal NF-κB activation, but little is known about the responsible substrate(s). Here

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38f7c37e997b3f63cd546f7424e39a64
https://doi.org/10.1073/pnas.1105020108

The Fanconi Anemia Protein FANCM Can Promote Branch Migration of Holliday Junctions and Replication Forks

Autor: Kerstin Gari, Angelos Constantinou, Andrzej Stasiak, Alicja Z. Stasiak, Chantal Décaillet

Publikováno v: Molecular Cell. 29:141-148

Fanconi anemia (FA) is a genetically heterogeneous cancer-prone disorder associated with chromosomal instability and cellular hypersensitivity to DNA crosslinking agents. The FA pathway is suspected to play a crucial role in the cellular response to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e89d6e7f6ba322a0e3c0f12423eb2cf8
https://doi.org/10.1016/j.molcel.2007.11.032

A Histone-Fold Complex and FANCM Form a Conserved DNA-Remodeling Complex to Maintain Genome Stability

Autor: Hans Joenje, Ti Lin, Parameswary A. Muniandy, Jurgen Steltenpool, Chantal Décaillet, Mathieu Delannoy, Stacie Stone, Ranjan Sen, Hansen Du, Anneke B. Oostra, Alicja Z. Stasiak, Lei Li, Christopher L. Woodcock, Xi Shen, Johan P. de Winter, Detlev Schindler, Kyungjae Myung, Maureen E. Hoatlin, Michael M. Seidman, Weidong Wang, Andrzej Stasiak, Chen Ling, Danielle L. Daee, Fekret Osman, Angelos Constantinou, Beatrice Schuster, Zhijiang Yan, Matthew C. Whitby

Publikováno v: Molecular Cell, 37(6), 865-878. Cell Press
Molecular Cell, vol. 37, no. 6, pp. 865-878
Yan, Z J, Delannoy, M, Ling, C, Daee, D, Osman, F, Muniandy, P A, Shen, X, Oostra, A B, Du, H S, Steltenpool, J, Lin, T, Schuster, B, Decaillet, C, Stasiak, A, Stasiak, A Z, Stone, S, Hoatlin, M E, Schindler, D, Woodcock, C L, Joenje, H, Sen, R, de Winter, J P, Li, L, Seidman, M M, Whitby, M C, Myung, K, Constantinou, A & Wang, W 2010, ' A Histone-Fold Complex and FANCM Form a Conserved DNA-Remodeling Complex to Maintain Genome Stability ', Molecular Cell, vol. 37, no. 6, pp. 865-878 . https://doi.org/10.1016/j.molcel.2010.01.039

FANCM remodels branched DNA structures and plays essential roles in the cellular response to DNA replication stress. Here, we show that FANCM forms a conserved DNA-remodeling complex with a histone-fold heterodimer, MHF. We find that MHF stimulates D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0e52e06ce7ba2dc6840b22b8db4b412
https://research.vumc.nl/en/publications/8013b764-49bb-42a8-8561-eb8e28fa2d78