ArticleJournal of molecular recognition : JMR
Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation.
Article in Journal of molecular recognition : JMR. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Tumour initiated purinergic signalling promotes cardiomyocyte RBFOX1 degradation and cardiotoxicity from DNA damaging anticancer agents.Nature communications · 2025Article
- Molecular functions of HAX1 during disease progress.Virus genes · 2024Review
- Review
- Grb7 protein RA domain oligomerization.Journal of molecular recognition : JMR · 2017Article
- Grb7 and Hax1 may colocalize partially to mitochondria in EGF-treated SKBR3 cells and their interaction can affect Caspase3 cleavage of Hax1.Journal of molecular recognition : JMR · 2016Article
- Hax-1 is required for Rac1-Cortactin interaction and ovarian carcinoma cell migration.Genes & cancer · 2014Article
- Grb7 and Filamin-a associate and are colocalized to cell membrane ruffles upon EGF stimulation.Journal of molecular recognition : JMR · 2013Article
- Dimerization in the Grb7 protein.Journal of molecular recognition : JMR · 2012Article
- The role of molecular microtubule motors and the microtubule cytoskeleton in stress granule dynamics.International journal of cell biology · 2011Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Adaptor proteins mediate signal transduction from cell surface receptors to downstream signaling pathways. The Grb7 protein family of adaptor proteins is constituted by Grb7, Grb10, and Grb14. This protein family has been shown to be overexpressed in certain cancers and cancer cell lines. Grb7-mediated cell migration has been shown to proceed through a focal adhesion kinase (FAK)/Grb7 pathway, although the specific participants downstream of Grb7 in cell migration signaling have not been fully determined. In this study, we report that Grb7 interacts with Hax-1, a cytoskeletal-associated protein found overexpressed in metastatic tumors and cancer cell lines. Additionally, in yeast 2-hybrid assays, we show that the interaction is specific to the Grb7-RA and -PH domains. We have also demonstrated that full-length Grb7 and Hax-1 interact in mammalian cells and that Grb7 is tyrosine phosphorylated. Isothermal titration calorimetry measurements demonstrate the Grb7-RA-PH domains bind to the Grb7-SH2 domain with micromolar affinity, suggesting full-length Grb7 can exist in a head-to-tail conformational state that could serve a self-regulatory function.
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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.