MassIVE MSV000089179

Partial Public

Human Caspase-4 and -5 proteins have different expression profiles and biological functions

Description

Inflammatory caspases are the central components of inflammasomes, among which the mouse Caspase-11 and human Caspase-4 and -5 are the core modules of non-canonical inflammasomes and function as the innate immune pattern recognition receptors (PRRs) for intracellular bacterial lipopolysaccharide (LPS). To answer the question why human encodes two proteins (Caspase-4 and -5) for this biological process instead of one (Caspase-11) in mouse, we examined the expression profiles and biological functions of human Caspase-4 and -5. In primary cultures of human monocyte-derived macrophages (MDMs) and colonic intestinal epithelial cell (IEC) organoids, we demonstrated that while Caspase-4 broadly expresses in different cell types, Caspase-5 is enriched in IECs and macrophages. To explore the biological roles of Caspase-5 in human IECs, we performed biotin proximity labeling assay to identify Caspase-5 associated proteins. Caspase-5a was fused with BioID2, a biotin ligase that indiscriminately biotinylate spatially close proteins, and expressed in human colonic organoids. Biotinylated proteins were then isolated and identified by protein mass spectrometry (MS). Intriguingly, all the three disheveled proteins in human (DVL1/2/3) were among the top identified targets (ranked by peptide-spectrum match (PSM)). [doi:10.25345/C59C6S472] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Caspase-5 ; proximity labeling

Contact

Principal Investigators:
(in alphabetical order)
Beatrix Ueberheide, New York University School of Medicine, USA
Submitting User: Trixi
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Experimental Design
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Identification Results
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Quantification Results
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct peptide sequences (including modified variants or peptidoforms) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

"N/A" means no results of this type were submitted.
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