ArticleBiochemical and biophysical research communications2018
Caspase-1 regulates cellular trafficking via cleavage of the Rab7 adaptor protein RILP.
Article in Biochemical and biophysical research communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- The Arg/N-degron pathway mediates the secretion of apoptotic exosomes under oxidative stress in cancer cell.iScience · 2025Article
- RILP cleavage links an inflammatory state to enhanced tau propagation in a cell culture model of Alzheimer's disease.Molecular biology of the cell · 2025Article
- TRIM25 dictates selective miRNA loading into extracellular vesicles during inflammation.Scientific reports · 2023Article
- The Early Secretory Pathway Is Crucial for Multiple Aspects of the Hepatitis C Virus Life Cycle.Journal of virology · 2023Article
- Inflammatory macrophage to hepatocyte signals can be prevented by extracellular vesicle reprogramming.Journal of cell science · 2023Article
- Kakonein restores hyperglycemia-induced macrophage digestion dysfunction through regulation of cathepsin B-dependent NLRP3 inflammasome activation.Journal of leukocyte biology · 2022Article
- The RNA binding protein FMR1 controls selective exosomal miRNA cargo loading during inflammation.The Journal of cell biology · 2020Article
- Hepatitis C virus infection increases autophagosome stability by suppressing lysosomal fusion through an Arl8b-dependent mechanism.The Journal of biological chemistry · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular trafficking is a tightly regulated cellular process, mediated in part by Rab GTPases and their corresponding effector proteins. Viruses have evolved mechanisms to hijack these processes to promote their lifecycles. Here we describe a mechanism by which cleavage of the Rab7 adaptor protein, RILP (Rab interacting lysosomal protein) is induced by viral infection. We report that RILP is directly cleaved by caspase-1 and we have identified a novel caspase-1 recognition site at aspartic acid 75 within the RILP sequence. Alanine substitution at D75 blocks caspase-1-mediated RILP cleavage. Full-length RILP localizes in a tight vesicular structure near the perinuclear region while the cleaved form of RILP re-distributes throughout the cytoplasm. However, cleavage alone was insufficient to re-localize RILP to the cellular periphery and re-localization required specific phosphorylation events near the caspase-1 recognition site. The combination of cleavage and phosphorylation were both needed for release from the dynein component p150
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Registered trials
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