Publications by authors named "M Monetti"
Unlabelled: The fission yeast regulon genes , , and -encoding a cell surface-associated acid phosphatase (Pho1), a plasma membrane inorganic phosphate transporter (Pho84), and a plasma membrane glycerophosphocholine transporter (Tgp1)-are strongly upregulated in response to acute phosphate starvation, as are the and genes that encode putative 5'-nucleotidase paralogs of the binuclear metallophosphoesterase enzyme superfamily. Via proteomic analysis of the medium harvested from phosphate-replete and phosphate-starved fission yeast, we define a starvation secretome that includes SPBPB2B2.06c (renamed Efn1, for xtracellular ive-prime ucleotidase), SPAC1039.
View Article and Find Full Text PDFRecent studies have identified a family of rod-shaped proteins which includes VPS13 and ATG2 and are thought to mediate unidirectional lipid transport at intracellular membrane contacts by a bridge-like mechanism. Here, we show that one such protein, BLTP3A/UHRF1BP1, associates with VAMP7-positive vesicles via its C-terminal region and anchors them to lysosomes via the binding of its chorein domain containing N-terminal region to Rab7. Upon damage of lysosomal membranes and resulting mATG8 recruitment to their surface by CASM, BLTP3A first dissociates from lysosomes but then reassociates with them via an interaction of its LIR motif with mATG8.
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- The study investigates how the chromatin and protein expressions of colonic epithelial cells differ between healthy individuals and patients with ulcerative colitis (UC), highlighting the role of epithelial dysfunction in UC pathology.
- Researchers sorted and analyzed epithelial cells from colon biopsies of healthy controls and UC patients to uncover these differences in proteome and chromatin accessibility.
- Results show significant protein elevation linked to inflammation in UC, with a notable reduction of the water channel aquaporin 8, indicating specific epigenetic mechanisms that influence protein expression in health vs. disease.
Article Synopsis
- Mutations in the SF3B1 gene are prevalent in various cancers and lead to incorrect RNA splicing, but there are currently no treatments to fix these issues.
- Researchers discovered that the protein GPATCH8 is essential for the abnormal splicing caused by mutant SF3B1 and plays a key role in maintaining proper RNA processing.
- By silencing GPATCH8, they found that it corrected many of the splicing errors and improved blood cell formation in models of SF3B1-mutant cancers, suggesting a potential therapeutic approach.
Regulation of glucose transport, which is central for control of whole-body metabolism, is determined by the amount of GLUT4 glucose transporter (also known as SLC2A4) in the plasma membrane (PM) of fat and muscle cells. Physiologic signals [such as activated insulin receptor or AMP-activated protein kinase (AMPK)] increase PM GLUT4. Here, we show that the distribution of GLUT4 between the PM and interior of human muscle cells is dynamically maintained, and that AMPK promotes PM redistribution of GLUT4 by regulating exocytosis and endocytosis.
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