ArticleJournal of cell science2010
Sequential and gamma-secretase-dependent processing of the betacellulin precursor generates a palmitoylated intracellular-domain fragment that inhibits cell growth.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- zDHHC-Mediated S-Palmitoylation in Skin Health and Its Targeting as a Treatment Perspective.International journal of molecular sciences · 2025Review
- Fatty Acids: An Insight into the Pathogenesis of Neurodegenerative Diseases and Therapeutic Potential.International journal of molecular sciences · 2022Review
- BTC as a Novel Biomarker Contributing to EMTFrontiers in genetics · 2022Article
- Palmitic Acid: Physiological Role, Metabolism and Nutritional Implications.Frontiers in physiology · 2017Review
- Membrane-Tethered Intracellular Domain of Amphiregulin Promotes Keratinocyte Proliferation.The Journal of investigative dermatology · 2016Article
- Induction of lateral lumens through disruption of a monoleucine-based basolateral-sorting motif in betacellulin.Journal of cell science · 2015Article
- Trafficking of epidermal growth factor receptor ligands in polarized epithelial cells.Annual review of physiology · 2014Review
- Receptor tyrosine kinases in the nucleus.Cold Spring Harbor perspectives in biology · 2013Review
- The Coxsackievirus and Adenovirus Receptor (CAR) undergoes ectodomain shedding and regulated intramembrane proteolysis (RIP).PloS one · 2013Article
- Heparin-binding EGF-like growth factor promotes epithelial-mesenchymal transition in human keratinocytes.The Journal of investigative dermatology · 2012Article
- NAC1 is an actin-binding protein that is essential for effective cytokinesis in cancer cells.Cancer research · 2012Article
- Epidermal growth factor cytoplasmic domain affects ErbB protein degradation by the lysosomal and ubiquitin-proteasome pathway in human cancer cells.Neoplasia (New York, N.Y.) · 2012Article
- Cell surface annexins regulate ADAM-mediated ectodomain shedding of proamphiregulin.Molecular biology of the cell · 2012Article
- The many substrates of presenilin/γ-secretase.Journal of Alzheimer's disease : JAD · 2011Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Betacellulin (BTC) belongs to the family of epidermal growth factor (EGF)-like growth factors that are expressed as transmembrane precursors and undergo proteolytic ectodomain shedding to release soluble mature ligands. BTC is a dual-specificity ligand for ErbB1 and ErbB4 receptors, and can activate unique signal-transduction pathways that are beneficial for the function, survival and regeneration of pancreatic beta-cells. We have previously shown that BTC precursor (proBTC) is cleaved by ADAM10 to generate soluble ligand and a stable, transmembrane remnant (BTC-CTF). In this study, we analyzed the fate of the BTC-CTF in greater detail. We demonstrated that proBTC is cleaved by ADAM10 to produce BTC-CTF, which then undergoes intramembrane processing by presenilin-1- and/or presenilin-2-dependent gamma-secretase to generate an intracellular-domain fragment (BTC-ICD). We found that the proBTC cytoplasmic domain is palmitoylated and that palmitoylation is not required for ADAM10-dependent cleavage but is necessary for the stability and gamma-secretase-dependent processing of BTC-CTF to generate BTC-ICD. Additionally, palmitoylation is required for nuclear-membrane localization of BTC-ICD, as demonstrated by the redistribution of non-palmitoylated BTC-ICD mutant to the nucleoplasm. Importantly, a novel receptor-independent role for BTC-ICD signaling is suggested by the ability of BTC-ICD to inhibit cell growth in vitro.
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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.