ArticleAutophagy2022
When acidic residues do not mimic phosphorylation: high-affinity binding of the reticulophagy receptor TEX264 to LC3/GABARAP.
Article in Autophagy, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 5 citations in OpenAlex.
- The multifaceted functions of selective autophagy in cancer: molecular basis, consequences, and clinical prospects.Molecular cancer · 2026Review
- Endoplasmic reticulum autophagy in inflammatory diseases.Frontiers in immunology · 2026Review
- The LC3-interacting region of NBR1 is a protein interaction hub enabling optimal flux.The Journal of cell biology · 2025Article
- The LC3-interacting region of NBR1 is a protein interaction hub enabling optimal flux.bioRxiv : the preprint server for biology · 2024Article
- UVRAG cooperates with cargo receptors to assemble the ER-phagy site.The EMBO journal · 2023Article
- TNIP1 inhibits selective autophagy via bipartite interaction with LC3/GABARAP and TAX1BP1.Molecular cell · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Substrates that are selected for degradation by autophagy interact in more complex eukaryotes with Atg8-family proteins via the LC3-interacting region (LIR) that is often preceded by either acidic residues or phosphorylated serine or threonine. These upstream amino acid residues increase the binding affinity of the LIR motif to its binding site on the surface of LC3/GABARAP. It is not fully understood whether or how phosphorylation functionally replaces acidic residues in the LIR-Atg8-family protein interactions. A recent study by Chino et al. discussed in this article analyzed the phosphorylation of two serine residues upstream of the LIR motif in TEX264, a reticulophagy receptor that exhibits a high binding affinity to LC3/GABARAP proteins. The authors found a structural basis for the high-affinity interaction yielded by phosphorylation but not by an acidic residue in place of phosphoserine. Furthermore, finding that phosphorylation of TEX264 generates its high binding affinity to Atg8-family proteins uncovers a mechanistic alternative to that utilized by other reticulophagy receptors when they interact with LC3/GABARAP.
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Registered trials
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 OpenQuestion graph.