ArticlePloS one2009
Structure-function analysis of nucleolin and ErbB receptors interactions.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Nucleolin‑based targeting strategies in cancer treatment: Focus on cancer immunotherapy (Review).International journal of molecular medicine · 2023Pooled it
- Nucleolar origins: challenging perspectives on evolution and function.Open biology · 2025Review
- Identification of Nucleolin as a Novel AEG-1-Interacting Protein in Breast Cancer via Interactome Profiling.Cancers · 2021Article
- Growth Factor Midkine Aggravates Pulmonary Arterial Hypertension via Surface Nucleolin.Scientific reports · 2020Article
- Altered immunoreactivity of ErbB4, a causative gene product for ALS19, in the spinal cord of patients with sporadic ALS.Neuropathology : official journal of the Japanese Society of Neuropathology · 2019Article
- The characterization, management, and future considerations for ErbB-family TKI-associated diarrhea.Breast cancer research and treatment · 2019Review
- Investigation of Different Molecular Weight Fucoidan Fractions Derived from New ZealandMarine drugs · 2018Article
- The long non-coding RNA CYTOR drives colorectal cancer progression by interacting with NCL and Sam68.Molecular cancer · 2018Article
- Nucleolin and ErbB2 inhibition reduces tumorigenicity of ErbB2-positive breast cancer.Cell death & disease · 2018Article
- Phosphoproteomics Reveals HMGA1, a CK2 Substrate, as a Drug-Resistant Target in Non-Small Cell Lung Cancer.Scientific reports · 2017Article
- Nucleolin-binding by ErbB2 enhances tumorigenicity of ErbB2-positive breast cancer.Oncotarget · 2016Article
- Mechanistic studies of anticancer aptamer AS1411 reveal a novel role for nucleolin in regulating Rac1 activation.Molecular oncology · 2015Article
- Nucleolin promotes TGF-β signaling initiation via TGF-β receptor I in glioblastoma.Journal of molecular neuroscience : MN · 2015Article
- Interfering with the interaction between ErbB1, nucleolin and Ras as a potential treatment for glioblastoma.Oncotarget · 2014Article
- Cellular stress induces Bax-regulated nuclear bubble budding and rupture followed by nuclear protein release.Nucleus (Austin, Tex.) · 2014Article
- Identification of nucleolin as a lipid-raft-dependent β1-integrin-interacting protein in A375 cell migration.Molecules and cells · 2013Article
- In vivo NCL targeting affects breast cancer aggressiveness through miRNA regulation.The Journal of experimental medicine · 2013Article
- Disrupting the oncogenic synergism between nucleolin and Ras results in cell growth inhibition and cell death.PloS one · 2013Article
- The atypical histone macroH2A1.2 interacts with HER-2 protein in cancer cells.The Journal of biological chemistry · 2012Article
- Nuclear translocation of type I transforming growth factor β receptor confers a novel function in RNA processing.Molecular and cellular biology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe ErbB receptor tyrosine kinases and nucleolin are major contributors to malignant transformation. Recently we have found that cell-surface ErbB receptors interact with nucleolin via their cytoplasmic tail. Overexpression of ErbB1 and nucleolin leads to receptor phosphorylation, dimerization and anchorage independent growth. METHODOLOGY/PRINCIPAL
findingsIn the present study we explored the regions of nucleolin and ErbB responsible for their interaction. Using mutational analyses, we addressed the structure-function relationship of the interaction between ErbB1 and nucleolin. We identified the ErbB1 nuclear localization domain as nucleolin interacting region. This region is important for nucleolin-associated receptor activation. Notably, though the tyrosine kinase domain is important for nucleolin-associated receptor activation, it is not involved in nucleolin/ErbB interactions. In addition, we demonstrated that the 212 c-terminal portion of nucleolin is imperative for the interaction with ErbB1 and ErbB4. This region of nucleolin is sufficient to induce ErbB1 dimerization, phosphorylation and growth in soft agar. CONCLUSIONS/SIGNIFICANCE: The oncogenic potential of ErbB depends on receptor levels and activation. Nucleolin affects ErbB dimerization and activation leading to enhanced cell growth. The C-terminal region of nucleolin and the ErbB1 NLS-domain mediate this interaction. Moreover, when the C-terminal 212 amino acids region of nucleolin is expressed with ErbB1, it can enhance anchorage independent cell growth. Taken together these results offer new insight into the role of ErbB1 and nucleolin interaction in malignant cells.
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