ArticleThe Journal of biological chemistry2025
ADP ribosylation factor-like GTPase 6-interacting protein 5 (Arl6IP5) is an ER membrane-shaping protein that modulates ER-phagy.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A highly abundant circular RNA from the RMST locus plays a role in posterior fossa ependymoma pathogenesis.Brain pathology (Zurich, Switzerland) · 2026Article
- Endoplasmic reticulum autophagy in inflammatory diseases.Frontiers in immunology · 2026Review
- ADP ribosylation factor-like GTPase 6-interacting protein 5 (ARL6IP5): a prenylated Rab acceptor protein 1 (PRA1) family protein that shapes the ER membrane and regulates ER-phagy.Autophagy reports · 2025Article
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER) is the membrane-bound organelle characterized by the reticular network of tubules. It is well established that the ER tubules are shaped by ER membrane proteins containing the conserved reticulon-homology domain (RHD). Membrane shaping by the RHD-containing proteins is also involved in the regulation of ER-phagy, selective autophagy of the ER. However, it remains unclear whether there exists ER membrane-shaping proteins other than the RHD-containing proteins. In this study, we characterize Arl6IP5, an ER membrane protein containing the conserved PRA1 domain, as an ER membrane-shaping protein. Upon overexpression, Arl6IP5 induces the extensive network of the ER tubules and constricts the ER membrane as judged by exclusion of a luminal ER enzyme from the ER tubules. The membrane constriction by Arl6IP5 allows the cells to maintain the tubular ER network in the absence of microtubules. siRNA-mediated knockdown of Arl6IP5 impairs the ER morphology, and the phenotype of the Arl6IP5 knockdown cells is rescued by exogenous expression of Arl6IP1, an RHD-containing protein. Furthermore, exogenous expression of Arl6IP5 rescues the phenotype of Arl6IP1 knockdown cells, and the PRA1 domain is sufficient to rescue it. Upon disruption of the possible short hairpin structures of the PRA1 domain, Arl6IP5 abolishes membrane constriction. The siRNA-mediated knockdown of Arl6IP5 impairs flux of the ER-phagy mediated by FAM134B. These results indicate that Arl6IP5 acts as an ER membrane-shaping protein involved in the regulation of ER-phagy, implying that the PRA1 domain may serve as a general membrane-shaping unit other than the RHD.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.