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Cited by 30Cell Adhesion Molecules ResearchProtein Kinase Regulation and GTPase SignalingGrowth Hormone and Insulin-like Growth Factors

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Targeting of the protein interaction site between FAK and IGF-1R

Open access
Zheng, Donghang, Kurenova, Elena, Ucar, Deniz, Golubovskaya, Vita, Magis, Andrew, Ostrov, David, Cance, William G., Hochwald, Steven N.·2009·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2009.07.156PMC PMC2742998
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Abstract

The interaction of focal adhesion kinase (FAK) and insulin-like growth factor-1 receptor (IGF-1R) plays an important role in cancer cell survival. Targeting this interaction with small molecule drugs could be a novel strategy in cancer therapy. By a series of pull-down assays using GST-tagged FAK fragments and His-tagged IGF-1R intracellular fragments, we showed that the FAK-NT2 (a.a. 127-243) domain directly interacts with the N-terminal part of the IGF-1R intracellular domain. Overexpressed FAK-NT2 domain was also shown to co-localize with IGF-1R in pancreatic cells. Computational modeling was used to predict the binding configuration of these two domains and to screen for small molecules binding to the interaction site. This strategy successfully identified a lead compound that disrupts FAK/IGF-1R interaction.

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Crossref · 10.1016/j.bbrc.2009.07.156

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  • The FERM domain of FAK directly binds to the β-subunit of IGF-1R, housing the intracellular tyrosine kinase domain, thereby activating FAK in human cells.

    “The FERM domain of FAK directly binds to the β -subunit of IGF-1R, housing the intracellular tyrosine kinase domain, thereby activating FAK in human cells [42, 43].”

    From Epithelial-mesenchymal transition status is a remarkable biomarker for the combination treatment with avutometinib and defactinib in KRAS-mutated non-small cell lung cancer (2024) · cites this paper as [42]

    The Results section (‘Direct interaction of FAK-NT2 domain and IGF-1R intracellular domain in vitro’; page not available) shows direct binding between FAK-NT2, part of the FERM domain, and an IGF-1R intracellular fragment containing the kinase domain. The Introduction identifies the kinase domain as part of the IGF-1R β-subunit. The Discussion reports co-localization in pancreatic cancer cells, but does not show that this binding activates FAK in human cells. (LLM, conf=0.88)

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Research works printed but not linked: 1

  1. S.N. Hochwald, V.M. Golubovskaya, FAK as a target for cancer therapy, Gene Ther. Mol. Biol., in press.

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Metadata

Authors
Zheng, D., Kurenova, E., Ucar, D., Golubovskaya, V., Magis, A., Ostrov, D., Cance, W. G., & Hochwald, S. N.
Affiliations
  • University of Florida (US)
  • Roswell Park Comprehensive Cancer Center (US)
Corresponding author
Hochwald, Steven N.
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2009-10
Volume
388
Issue
2
Pages
301-305
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2009.07.156
PMC
PMC2742998
OpenAlex
W2069525853
Cited by
30
References
42
Citations by year
2024: 1 · 2023: 1 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 2 · 2016: 4 · 2015: 2 · 2013: 3 · 2012: 5
FWCI
3.44
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Cancer Institute (R01CA065910, K08CA113766, CA113766)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
Keywords
focal adhesion kinase, IGF-1 receptor, protein-protein interaction, small molecule inhibitors, tumor cell survival, pancreatic cancer cells, lead compound identification
MeSH terms
Humans, Models, Molecular, Pancreatic Neoplasms, Protein Conformation, Receptor, IGF Type 1, Protein Interaction Mapping, Cell Line, Tumor, Focal Adhesion Kinase 1, Protein Interaction Domains and Motifs

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