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Bargfrede, S.

Publications and source records attributed to Bargfrede, S..

2 recordsLinked to original sources

A VHL-1/HIF-1/SQRD1/COL-88 axis links extracellular matrix formation with longevity in Caenorhabditis elegans

The extracellular matrix (ECM) is a pivotal three-dimensional network crucial for tissue organization, cellular communication, and fundamental cellular processes, where collagens are the major chemical entity in amount. ECM deregulation is directly involved with several pathologies, such as tumour growth and invasiveness, atherosclerosis, and diabetic nephropathy. Mutations in the von Hippel-Lindau tumour suppressor (pVHL) cause VHL syndrome, a multi-tumour syndrome commonly associated with clear cell renal carcinoma (ccRCC). Loss of pVHL is associated with the activation of hypoxia-inducible factor (HIF) signaling. Mutation of VHL-1 in the nematode Canorhabditis elegans has been shown to increase lifespan and stress resistance. Interestingly, considering recent findings on the involvement of collagens in the regulation of lifespan, we also observed these animals to show defects in body morphology in a HIF-1 dependent manner. Based on this finding, we established a link between HIF-1 activation upon loss of VHL-1 and ECM defects associated with alterations in collagen expression. An RNAi screen examining genes upregulated in vhl-1 mutant worms revealed the sulfide quinone oxidoreductase sqrd-1 to mediate the change in body morphology. SQRD-1 is essential to the HIF-1 dependent increase in several collagen genes. One of these genes, col-88, partly mediates both the impact of loss of VHL-1 on lifespan extension and body length. The downregulation of the uncharacterised col-88 partially restores lifespan extension and reduces body size of vhl-1/sqrd-1 to vhl-1(ok161) single mutant. This study contributes to the increasing body of evidence linking lifespan extension and the ECM and now implicates this axis in hypoxia-signaling. These findings are of special interest considering the role of ECM integrity in tumour growth and metastasis. Author SummaryThe extracellular matrix and its composing collagens are associated with a wide number of diseases, including cancer. The von Hippel-Lindau tumour suppressor (pVHL) is known to work by regulating the Hypoxia Inducible Factor (HIF) to help the organism to adapt to lack of oxygen. Mutations in pVHL are associated with clear cell renal carcinoma (ccRCC). Interestingly, a small number of studies have shown that pVHL can be directly associated with collagens, a function that is independent of its classical role regulating HIF. However, there is no further knowledge about which role the hypoxia pathway has when it comes to extracellular matrix formation and function, what would be useful since the invasiveness of cancers, such as ccRCC, are directly connected to their matrix/collagen composition. Here we observed that the model organism C. elegans has drastically different collagen composition and body size upon a mutation on its vhl-1 gene. Furthermore, a protein previously only known to be involved in sulfide metabolism, SQRD-1, connects body size and lifespan in this animal model, revealing a surprising link between the hypoxia pathway and sulfur metabolism to control lifespan. Further studies could target sulfur metabolism in ccRCC to modulate collagen production and tumour invasiveness.

genetics↗

JADE family proteins regulate proteasome abundance and activity

The JADE protein family (JADE1/2/3) has been implicated in a broad range of cellular functions, including WNT signaling, cell cycle control, regulated cell death, and transcriptional regulation through histone acetyltransferase complexes. All three paralogs share high sequence similarity and contain two PHD zinc finger domains. JADE1 has additionally been associated with cilia-related proteins and genetic disorders affecting kidney architecture and function. Despite their widespread expression, the molecular roles of JADE proteins remain incompletely understood. Here, we identify JADE proteins as regulators of proteasome abundance and activity. Using kidney cells as a model, we demonstrate that loss of any single JADE protein led to a marked upregulation of almost all components of the 26S proteasome. Regulation occurred at the post-translational level and was not the consequence of increased transcription. Consistent with a role for JADE proteins in regulating overall proteasomal abundance, JADE-deficient cells displayed elevated proteasomal activity, while ectopic expression of JADE1, JADE2, or JADE3 reduced proteasomal function. Co-immunoprecipitation experiments confirmed the interaction between JADE1 and multiple proteasomal subunits, supporting a direct role of JADE proteins in modulating proteasome turnover, stability and abundance. These findings reveal a novel function of JADE proteins in proteostasis and suggest that their previously reported cellular roles may, in part, be mediated through regulation of the ubiquitin-proteasome system.

cell biology↗