ArticleThe Journal of cell biology1998
Removal of the membrane-anchoring domain of epidermal growth factor leads to intracrine signaling and disruption of mammary epithelial cell organization.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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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Who cites it
21 citing papers in PubMed, 59 citations in OpenAlex.
- Analysis of the function of ADAM17 in iRhom2 curly-bare and tylosis with esophageal cancer mutant mice.Journal of cell science · 2023Article
- ADAM17-mediated EGFR ligand shedding directs macrophage-promoted cancer cell invasion.JCI insight · 2022Article
- Contribution of ADAM17 and related ADAMs in cardiovascular diseases.Cellular and molecular life sciences : CMLS · 2021Review
- The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site.The Journal of biological chemistry · 2015Article
- G protein-coupled receptor signalling in the cardiac nuclear membrane: evidence and possible roles in physiological and pathophysiological function.The Journal of physiology · 2012Review
- Transautocrine signaling by membrane neuregulins requires cell surface targeting, which is controlled by multiple domains.The Journal of biological chemistry · 2011Article
- Structure of the EGF receptor transactivation circuit integrates multiple signals with cell context.Molecular bioSystems · 2010Article
- ADAM-17: the enzyme that does it all.Critical reviews in biochemistry and molecular biology · 2010Review
- Rapid and sustained nuclear-cytoplasmic ERK oscillations induced by epidermal growth factor.Molecular systems biology · 2009Article
- The extracellular linker of pro-neuregulin-alpha2c is required for efficient sorting and juxtacrine function.Molecular biology of the cell · 2007Article
- Activation of the epidermal growth factor (EGF) receptor induces formation of EGF receptor- and Grb2-containing clathrin-coated pits.Molecular and cellular biology · 2006Article
- The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane.Molecular biology of the cell · 2005Article
- The membrane-anchoring domain of epidermal growth factor receptor ligands dictates their ability to operate in juxtacrine mode.Molecular biology of the cell · 2005Article
- Ligand accumulation in autocrine cell cultures.Biophysical journal · 2005Article
- Cbl-dependent ubiquitination is required for progression of EGF receptors into clathrin-coated pits.Molecular biology of the cell · 2004Article
- Stochastic model of autocrine and paracrine signals in cell culture assays.Biophysical journal · 2003Article
- Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities.The Journal of cell biology · 2003Article
- Autocrine epidermal growth factor signaling stimulates directionally persistent mammary epithelial cell migration.The Journal of cell biology · 2001Article
- Spatial range of autocrine signaling: modeling and computational analysis.Biophysical journal · 2001Article
- Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking.Molecular biology of the cell · 2001Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Autocrine EGF-receptor (EGFR) ligands are normally made as membrane-anchored precursors that are proteolytically processed to yield mature, soluble peptides. To explore the function of the membrane-anchoring domain of EGF, we expressed artificial EGF genes either with or without this structure in human mammary epithelial cells (HMEC). These cells require activation of the EGFR for cell proliferation. We found that HMEC expressing high levels of membrane- anchored EGF grew at a maximal rate that was not increased by exogenous EGF, but could be inhibited by anti-EGFR antibodies. In contrast, when cells expressed EGF lacking the membrane-anchoring domain (sEGF), their proliferation rate, growth at clonal densities, and receptor substrate phosphorylation were not affected by anti-EGFR antibodies. The sEGF was found to be colocalized with the EGFR within small cytoplasmic vesicles. It thus appears that removal of the membrane-anchoring domain converts autocrine to intracrine signaling. Significantly, sEGF inhibited the organization of HMEC on Matrigel, suggesting that spatial restriction of EGF access to its receptor is necessary for organization. Our results indicate that an important role of the membrane-anchoring domain of EGFR ligands is to restrict the cellular compartments in which the receptor is activated.
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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.