ArticleMolecular and cellular biology2001
Proteolysis of the docking protein HEF1 and implications for focal adhesion dynamics.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
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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
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.
- The Prognostic Significance of NEDD9 Expression in Human Cancers: A Systematic Review, Meta-Analysis, and Omics Exploration.Technology in cancer research & treatmentPooled it
- Genome-Wide Detection of Copy Number Variations and Their Potential Association with Carcass and Meat Quality Traits in Pingliang Red Cattle.International journal of molecular sciences · 2024Article
- NEDD9 Restrains dsDNA Damage Response during Non-Small Cell Lung Cancer (NSCLC) Progression.Cancers · 2022Article
- NEDD9 Is a Novel and Modifiable Mediator of Platelet-Endothelial Adhesion in the Pulmonary Circulation.American journal of respiratory and critical care medicine · 2021Article
- Melatonin Inhibits the Progression of Oral Squamous Cell CarcinomaFrontiers in oncology · 2020Article
- NEDD9 overexpression predicts poor prognosis in solid cancers: a meta-analysis.OncoTargets and therapy · 2019Review
- Differential transcriptional changes in human alveolar epithelial A549 cells exposed to airborne PMEnvironmental science and pollution research international · 2018Article
- Integration of Canonical and Noncanonical Pathways in TLR4 Signaling: Complex Regulation of the Wound Repair Program.Advances in wound care · 2017Review
- Dual Targeting of Mesenchymal and Amoeboid Motility Hinders Metastatic Behavior.Molecular cancer research : MCR · 2017Article
- The expressions of NEDD9 and E-cadherin correlate with metastasis and poor prognosis in triple-negative breast cancer patients.OncoTargets and therapy · 2016Article
- Preclinical and clinical studies of the NEDD9 scaffold protein in cancer and other diseases.Gene · 2015Review
- Src kinase determines the dynamic exchange of the docking protein NEDD9 (neural precursor cell expressed developmentally down-regulated gene 9) at focal adhesions.The Journal of biological chemistry · 2014Article
- Nedd9 restrains renal cystogenesis in Pkd1-/- mice.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Overexpression of Nedd9 is a prognostic marker of human gastric cancer.Medical oncology (Northwood, London, England) · 2014Article
- NEDD9 overexpression correlates with the progression and prognosis in gastric carcinoma.Medical oncology (Northwood, London, England) · 2014Article
- A requirement for Nedd9 in luminal progenitor cells prior to mammary tumorigenesis in MMTV-HER2/ErbB2 mice.Oncogene · 2014Article
- siRNA Suppression of NEDD9 Inhibits Proliferation and Enhances Apoptosis in Renal Cell Carcinoma.Oncology research · 2014Article
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- Dual inhibition of SRC and Aurora kinases induces postmitotic attachment defects and cell death.Oncogene · 2012Article
- Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The dynamic regulation of focal adhesions is implicated in cellular processes of proliferation, differentiation, migration, and apoptosis. The focal adhesion-associated docking protein HEF1 is cleaved by caspases during both mitosis and apoptosis. Common to both of these cellular processes is the loss of focal adhesions, transiently during mitosis and permanently during apoptosis. The proteolytic processing of HEF1 during both mitosis and apoptosis therefore posits a general role for HEF1 as a sensor of altered adhesion states. In this study, we find that HEF1 undergoes proteolytic processing specifically in response to cellular detachment, while HEF1 proteolysis is prevented by specific integrin receptor ligation and focal adhesion formation. We show that overexpression of a C-terminal caspase-derived 28-kDa HEF1 peptide causes cellular rounding that is demonstrably separable from apoptosis. Mutation of the divergent helix-loop-helix motif found in 28-kDa HEF1 significantly reduces the induction of apoptosis by this peptide, while deletion of the amino-terminal 28 amino acids of 28-kDa HEF1 completely abrogates the induction of apoptosis. Conversely, these mutations have no effect on the rounding induced by 28-kDa HEF1. Finally, we detect a novel focal adhesion targeting domain located in the C terminus of HEF1 and show that this activity is necessary for HEF1-induced cell spreading. Together, these data suggest that proteolytic and other posttranslational modifications of HEF1 in response to loss of adhesion serve to modulate the disassembly of focal adhesions.
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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 OpenQuestion graph.