ArticleTraffic (Copenhagen, Denmark)2021
A highly conserved glutamic acid in ALFY inhibits membrane binding to aid in aggregate clearance.
Article in Traffic (Copenhagen, Denmark), 2021. 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, 10 citations in OpenAlex.
- The role of E3 ubiquitin ligases in selective types of macroautophagy.EMBO reports · 2026Review
- Article
- Macrophage WDFY3 mitigates autoimmunity by enhancing efferocytosis and suppressing T cell activation in mice.Nature communications · 2025Article
- Macrophage WDFY3, a protector against autoimmunity.bioRxiv : the preprint server for biology · 2024Article
- The evolving biology of cross-presentation.Seminars in immunology · 2023Review
- The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals.Membranes · 2022Article
- Longitudinal intronic RNA-Seq analysis of Parkinson's disease patients reveals disease-specific nascent transcription.Experimental biology and medicine (Maywood, N.J.) · 2022Article
- ALFY localizes to early endosomes and cellular protrusions to facilitate directional cell migration.Journal of cell science · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Autophagy-linked FYVE protein (ALFY) is a large, multidomain protein involved in the degradation of protein aggregates by selective autophagy. The C-terminal FYVE domain of ALFY has been shown to bind phosphatidylinositol 3-phosphate (PI(3)P); however, ALFY only partially colocalizes with other FYVE domains in cells. Thus, we asked if the FYVE domain of ALFY has distinct membrane binding properties compared to other FYVE domains and whether these properties might affect its function in vivo. We found that the FYVE domain of ALFY binds weakly to PI(3)P containing membranes in vitro. This weak binding is the result of a highly conserved glutamic acid within the membrane insertion loop in the FYVE domain of ALFY that is not present in any other human FYVE domain. In addition, not only does this glutamic acid reduce binding to membranes in vitro and inhibits its targeting to membranes in vivo, but it is also important for the ability of ALFY to clear protein aggregates.
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Registered trials
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