ArticleMolecular biology of the cell2012
The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 45 citations in OpenAlex.
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- The ubiquitin-binding protein ANKRD13A mediates VCP-dependent mitochondrial outer membrane rupture during PINK1/Parkin-mediated mitophagy.The Journal of biological chemistry · 2025Article
- The roles of non-coding RNAs (ncRNAs) in the function of leukemic stem cells (LSCs): a comprehensive review.Discover oncology · 2025Review
- K48- and K63-linked ubiquitin chain interactome reveals branch- and length-specific ubiquitin interactors.Life science alliance · 2024Article
- Biophysical interplay between extracellular matrix remodeling and hypoxia signaling in regulating cancer metastasis.Frontiers in cell and developmental biology · 2024Review
- p97/VCP targetsmSphere · 2023Article
- ANKRD26 is a new regulator of type I cytokine receptor signaling in normal and pathological hematopoiesis.Haematologica · 2023Article
- Triubiquitin Probes for Identification of Reader and Eraser Proteins of Branched Polyubiquitin Chains.ACS chemical biology · 2023Article
- Human papillomavirus integration perspective in small cell cervical carcinoma.Nature communications · 2022Article
- ANKRD13a controls early cell-death checkpoint by interacting with RIP1 independent of NF-κB.Cell death and differentiation · 2022Article
- LncRNA USP30-AS1 promotes the survival of acute myeloid leukemia cells by cis-regulating USP30 and ANKRD13A.Human cell · 2022Article
- Population Genetic Structure and Selection Signature Analysis of Beijing Black Pig.Frontiers in genetics · 2022Article
- Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling.Life science alliance · 2021Article
- Rare variants in the endocytic pathway are associated with Alzheimer's disease, its related phenotypes, and functional consequences.PLoS genetics · 2021Article
- Network analysis identifies DAPK3 as a potential biomarker for lymphatic invasion and colon adenocarcinoma prognosis.iScience · 2021Article
- The T cell CD6 receptor operates a multitask signalosome with opposite functions in T cell activation.The Journal of experimental medicine · 2021Article
- ANKRD22 is involved in the progression of prostate cancer.Oncology letters · 2019Article
- TRIAD3/RNF216 E3 ligase specifically synthesises K63-linked ubiquitin chains and is inactivated by mutations associated with Gordon Holmes syndrome.Cell death discovery · 2019Article
- Tandem UIMs confer Lys48 ubiquitin chain substrate preference to deubiquitinase USP25.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism of ubiquitin-dependent endocytosis of cell surface proteins is not completely understood. Here we examine the role of the ankyrin repeat domain (Ankrd) 13A, 13B, and 13D proteins, which constitute a functionally unknown family of ubiquitin-interacting motif (UIM)-bearing proteins, in the process. Stimulation of human HeLa cells with epidermal growth factor (EGF) rapidly induced direct binding of Ankrd 13 proteins to ubiquitinated EGF receptor (EGFR) via the UIMs. The binding was inhibited when the Ankrd 13 proteins underwent UIM-dependent monoubiquitination, suggesting that their activity is regulated by ubiquitination of themselves. Ankrd 13 proteins bound specifically to Lys-63-linked ubiquitin chains, which was consistent with a previous report that EGFR mainly undergoes Lys-63-linked polyubiquitination. Ankrd 13 proteins were anchored, via the central region and UIMs, to the plasma membrane, where they colocalized with EGFR. Finally, overexpression of wild-type as well as truncated-mutant Ankrd 13 proteins strongly inhibited rapid endocytosis of ubiquitinated EGFR from the surface in EGF-treated cells. We conclude that by binding to the Lys-63-linked polyubiquitin moiety of EGFR at the plasma membrane, Ankrd 13 proteins regulate the rapid internalization of ligand-activated EGFR.
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