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TMT10-TAILS for monitoring MALT1 substrate cleavage

ABSTRACT: We used TMT-TAILS to monitor MALT1 substrate cleavage in normal EBV B lymphocytes stimulated with PMA/ionomycin to evaluate kinetic profiles of MALT1 inhibitors

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Christopher M. Overall

PROVIDER: MSV000083026 | MassIVE | Thu Oct 11 16:16:00 BST 2018

SECONDARY ACCESSION(S): PXD008421

REPOSITORIES: MassIVE

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TMT10-TAILS for monitoring MALT1 substrate cleavage

Project description:We used TMT-TAILS to monitor MALT1 substrate cleavage in normal EBV B lymphocytes stimulated with PMA/ionomycin to evaluate kinetic profiles of MALT1 inhibitors

2018-10-02 | PXD008421 | Pride

TMT10-TAILS investigation of the proteolytic landscape in B cell activation

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Intestinal Differentiation Involves Cleavage of Histone H3 NTerminal Tails by Multiple Proteases

Project description:The proteolytic cleavage of histone tails, also termed histone clipping, has been described as a mechanism for permanent removal of post-translational modifications (PTMs) from histone proteins. Such activity has been ascribed to ensure regulatory function in key cellular processes such as differentiation, senescence and transcriptional control for which different histone-specific proteases has been described. However, all these studies were exclusively performed using cell lines cultured in vitro and no clear evidences that histone clipping is regulated in vivo has been reported. Here we show that histone H3 N-terminal tails undergo extensive cleavage in the differentiated cells of the villi fraction of the mouse intestinal epithelium. Combining biochemical methods, 3D organoids cultures and in vivo approaches, we demonstrate that intestinal H3 clipping is the result of multiple proteolytic activities. We identified Trypsins and Cathepsin L as specific H3 tail proteases active in small intestinal differentiated cells and showed that their proteolytic activity is differentially affected by the PTM pattern of histone H3 tails. Together, our findings provide in vivo evidences of H3 tail proteolysis in mammalian tissues directly linking H3 clipping to cell differentiation.

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TMT10-TAILS investigation of the proteolytic landscape in B cell activation

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Intestinal Differentiation Involves Cleavage of Histone H3 NTerminal Tails by Multiple Proteases

Project description:Intestinal Differentiation Involves Cleavage of Histone H3 NTerminal Tails by Multiple Proteases

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Translation of poly(A) tails leads to precise mRNA cleavage and widespread ribosome rescue

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Intestinal Differentiation Involves Cleavage of Histone H3 NTerminal Tails by Multiple Proteases

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Histone N-tails modulate sequence-specific positioning of nucleosomes

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