ArticleiScience2026
Annexin A6 controls multi-organelle contact site formation and endolysosomal positioning, and remodels the STARD3 interactome.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Annexin A6 Is a Novel Cytosolic Regulator of Multiple Inter-organelle Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.))Article
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Annexin A6 (ANXA6) regulates cholesterol transfer across membrane contact sites (MCSs) between late endosomes/lysosomes (LE/Lys) and the endoplasmic reticulum (ER) via the late endosomal StAR-related lipid transfer domain-3 (STARD3) transporter. Here, we describe a significant reduction of MCSs in ANXA6-depleted HeLa cells, which could be rescued by restoration of ANXA6 expression. Using AnxA6 as bait in BioID-based assays, we demonstrate that ANXA6 interacts with various tethers and bona fide MCS proteins that can modulate multi-organelle contacts. STARD3 interactors identified in BioID assays include the mitochondrial translocator protein (TSPO) and myosin heavy chain 9 (MYH9). Strikingly, reduced MCS formation in ANXA6-depleted cells was associated with changes in the STARD3 interactome that indicate altered MCS tethering functions of STARD3. Specifically, ANXA6 deficiency correlated with (1) altered positioning of STARD3-positive LE/Lys; (2) a new repertoire of cortical actin-binding proteins, including myosins interacting with STARD3; (3) and decreased microvillar structures and focal adhesions.
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Registered trials
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