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Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL3 domain in solution

Han, Xiao ; Levkovets, Maria ; Lesovoy, Dmitry ; Sun, Renhua ; Wallerstein, Johan LU ; Sandalova, Tatyana ; Agback, Tatyana ; Achour, Adnane ; Agback, Peter and Orekhov, Vladislav Yu. (2022) In Biomolecular NMR Assignments 16. p.363-371
Abstract
Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial 1H,... (More)
Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial 1H, 13C Ile/Val/Leu-Methyl resonance assignment of the monomeric apo form of the paracaspase-IgL3 domain of human MALT1. Our results provide a solid ground for future elucidation of both the three-dimensional structure and the dynamics of MALT1, key for adequate development of inhibitors, and a thorough molecular understanding of its function(s). (Less)
Abstract (Swedish)
Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial 1H, 13C... (More)
Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial 1H, 13C Ile/Val/Leu-Methyl resonance assignment of the monomeric apo form of the paracaspase-IgL3 domain of human MALT1. Our results provide a solid ground for future elucidation of both the three-dimensional structure and the dynamics of MALT1, key for adequate development of inhibitors, and a thorough molecular understanding of its function(s). (Less)
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publishing date
type
Contribution to journal
publication status
published
in
Biomolecular NMR Assignments
volume
16
pages
9 pages
publisher
Springer
external identifiers
  • scopus:85137920110
ISSN
1874-2718
DOI
10.1007/s12104-022-10105-3
language
English
LU publication?
no
id
d6b441f3-300e-49b8-824d-6c4b05d724bf
date added to LUP
2024-02-15 12:20:13
date last changed
2024-02-19 15:06:28
@article{d6b441f3-300e-49b8-824d-6c4b05d724bf,
  abstract     = {{Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial <sup>1</sup>H, <sup>13</sup>C Ile/Val/Leu-Methyl resonance assignment of the monomeric apo form of the paracaspase-IgL<sub>3</sub> domain of human MALT1. Our results provide a solid ground for future elucidation of both the three-dimensional structure and the dynamics of MALT1, key for adequate development of inhibitors, and a thorough molecular understanding of its function(s).}},
  author       = {{Han, Xiao and Levkovets, Maria and Lesovoy, Dmitry and Sun, Renhua and Wallerstein, Johan and Sandalova, Tatyana and Agback, Tatyana and Achour, Adnane and Agback, Peter and Orekhov, Vladislav Yu.}},
  issn         = {{1874-2718}},
  language     = {{eng}},
  month        = {{09}},
  pages        = {{363--371}},
  publisher    = {{Springer}},
  series       = {{Biomolecular NMR Assignments}},
  title        = {{Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL<sub>3</sub> domain in solution}},
  url          = {{http://dx.doi.org/10.1007/s12104-022-10105-3}},
  doi          = {{10.1007/s12104-022-10105-3}},
  volume       = {{16}},
  year         = {{2022}},
}