ArticleJournal of molecular recognition : JMR
The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- The roles of FHL2 in cancer.Clinical and experimental medicine · 2023Review
- Expression of the phagocytic receptors αFrontiers in immunology · 2022Article
- Article
- Direct Interaction between Calmodulin and the Grb7 RA-PH Domain.International journal of molecular sciences · 2020Article
- 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
- 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
- Water-refined solution structure of the human Grb7-SH2 domain in complex with the erbB2 receptor peptide pY1139.Protein and peptide letters · 2012Article
- Loops govern SH2 domain specificity by controlling access to binding pockets.Science signaling · 2010Article
- Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis.The Journal of biological chemistry · 2009Article
- Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation.Journal of molecular recognition : JMRArticle
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Grb7 is an adaptor molecule that can mediate signal transduction from multiple cell surface receptors to various downstream signaling pathways. Grb7, along with Grb10 and Grb14, make up the Grb7 protein family. This protein family has been shown to be overexpressed in certain cancers and cancer cell lines. Grb7 and a receptor tyrosine kinase (RTK), erbB2, are overexpressed in 20-30% of breast cancers. Grb7 overexpression has been linked to enhanced cell migration and metastasis, though the participants in these pathways have not been determined. In this study, we report that Grb7 interacts with four and half lim domains isoform 2 (FHL2), a transcription regulator with an important role in oncogenesis, including breast cancer. Additionally, in yeast 2-hybrid (Y2H) assays, we show that the interaction is specific to the Grb7 RA and PH domains. We have also demonstrated that full-length (FL) Grb7 and FHL2 interact in mammalian cells and that Grb7 must be tyrosine phosphorylated for this interaction to occur. Immunofluorescent microscopy demonstrates possible co-localization of Grb7 and FHL2. A model with supporting NMR evidence of Grb7 autoinhibition is proposed.
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