ArticleMolecular biology of the cell1998
Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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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
71 citing papers in PubMed, 189 citations in OpenAlex.
- Functional Analysis of Late-Onset Alzheimer's Disease Risk Genes inbioRxiv : the preprint server for biology · 2026Article
- The ILK-PINCH-parvin complex: a conserved primary adhesome regulating biological processes.Histochemistry and cell biology · 2025Review
- Revisiting nephrin signaling and its specialized effects on the uniquely adaptable podocyte.The Biochemical journal · 2025Review
- Distinct Requirements for Adaptor Proteins NCK1 and NCK2 in Mammary Gland Development.Journal of mammary gland biology and neoplasia · 2023Article
- PINCH-1 promotes IGF-1 receptor expression and skin cancer progression through inhibition of the GRB10-NEDD4 complex.Theranostics · 2022Article
- Genome-wide association study for systemic lupus erythematosus in an egyptian population.Frontiers in genetics · 2022Article
- PINCH1 Promotes Fibroblast Migration in Extracellular Matrices and Influences Their Mechanophenotype.Frontiers in cell and developmental biology · 2022Article
- A Case of Lung Adenocarcinoma Harboring a RareJTO clinical and research reports · 2021Article
- Review
- A Potential Role for Integrin-Linked Kinase in Colorectal Cancer Growth and Progression via Regulating Senescence and Immunity.Frontiers in genetics · 2021Review
- Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy.American journal of physiology. Cell physiology · 2019Review
- LIMS1 Promotes Pancreatic Cancer Cell Survival under Oxygen-Glucose Deprivation Conditions by Enhancing HIF1A Protein Translation.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019Article
- Integrin-Linked Kinase Signaling Promotes Cyst Growth and Fibrosis in Polycystic Kidney Disease.Journal of the American Society of Nephrology : JASN · 2017Article
- Molecular insights of Gas6/TAM in cancer development and therapy.Cell death & disease · 2017Review
- Evidence for Integrin - Venus Kinase Receptor 1 Alliance in the Ovary of Schistosoma mansoni Females Controlling Cell Survival.PLoS pathogens · 2017Article
- Review
- ILK-PI3K/AKT pathway participates in cutaneous wound contraction by regulating fibroblast migration and differentiation to myofibroblast.Laboratory investigation; a journal of technical methods and pathology · 2016Article
- Actin remodeling by Nck regulates endothelial lumen formation.Molecular biology of the cell · 2015Article
- Transcriptional Response to Acute Thermal Exposure in Juvenile Chinook Salmon Determined by RNAseq.G3 (Bethesda, Md.) · 2015Article
- The focal adhesion protein PINCH-1 associates with EPLIN at integrin adhesion sites.Journal of cell science · 2015Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Many of the protein-protein interactions that are essential for eukaryotic intracellular signal transduction are mediated by protein binding modules including SH2, SH3, and LIM domains. Nck is a SH3- and SH2-containing adaptor protein implicated in coordinating various signaling pathways, including those of growth factor receptors and cell adhesion receptors. We report here the identification, cloning, and characterization of a widely expressed, Nck-related adaptor protein termed Nck-2. Nck-2 comprises primarily three N-terminal SH3 domains and one C-terminal SH2 domain. We show that Nck-2 interacts with PINCH, a LIM-only protein implicated in integrin-linked kinase signaling. The PINCH-Nck-2 interaction is mediated by the fourth LIM domain of PINCH and the third SH3 domain of Nck-2. Furthermore, we show that Nck-2 is capable of recognizing several key components of growth factor receptor kinase-signaling pathways including EGF receptors, PDGF receptor-beta, and IRS-1. The association of Nck-2 with EGF receptors was regulated by EGF stimulation and involved largely the SH2 domain of Nck-2, although the SH3 domains of Nck-2 also contributed to the complex formation. The association of Nck-2 with PDGF receptor-beta was dependent on PDGF activation and was mediated solely by the SH2 domain of Nck-2. Additionally, we have detected a stable association between Nck-2 and IRS-1 that was mediated primarily via the second and third SH3 domain of Nck-2. Thus, Nck-2 associates with PINCH and components of different growth factor receptor-signaling pathways via distinct mechanisms. Finally, we provide evidence indicating that a fraction of the Nck-2 and/or Nck-1 proteins are associated with the cytoskeleton. These results identify a novel Nck-related SH2- and SH3-domain-containing protein and suggest that it may function as an adaptor protein connecting the growth factor receptor-signaling pathways with the integrin-signaling pathways.
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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.