The p130Cas-Crk/CrkL Axis: A therapeutic target for invasive cancers unveiled by collaboration among p130Cas, Crk, and CrkL
Open accessAbstract
Numerous studies have documented the involvement of p130Cas (Crk-associated substrate) in a wide range of cellular processes across different types of cells. These processes encompass cell transformation, the connection between the extracellular matrix and the actin cytoskeleton, cell migration and invasion, and cardiovascular development. Moreover, p130Cas has been associated with the regulation of various physiological processes, including mammary, bone, brain, muscle, and liver homeostasis. The diverse functions of p130Cas can be attributed to its possession of multiple protein–protein interaction domains, which sets it apart as a unique class of adaptor protein. It is well established that p130Cas interacts critically with the CT10 regulator of kinase (Crk) adaptor protein family members, including CrkII, CrkI, and Crk-like (CrkL), which is the basis for the naming of the Cas family. The Crk family proteins play a crucial role in integrating signals from various sources, such as growth factors, extracellular matrix molecules, bacterial pathogens, and apoptotic cells. An increasing body of evidence suggests that the dysregulation of Crk family proteins is linked to various human diseases, including cancer and increased susceptibility to pathogen infections. This review focuses primarily on the structural and functional aspects of the interaction between p130Cas and the Crk family proteins, providing insights into how these proteins regulate specific signaling events. Furthermore, we delve into the functions of p130Cas and the Crk family proteins in both normal and tumor cells to gain a comprehensive understanding of their collaborative roles in cellular physiology and pathology. This review demonstrates that tumor cell migration and invasion are the two cellular functions that have been studied the most for the p130Cas-Crk/CrkL axis. Understanding the tumor cell migration and invasion that require both p130Cas and Crk/CrkL is necessary to further evaluate the role of the p130Cas-Crk/CrkL axis in cancer. Establishing the contribution of the p130Cas-Crk/CrkL axis to cancer will facilitate the development of cancer drugs targeting the axis to inhibit cancer cell dissemination and improve patient outcomes.
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17% of the 93 differentially phosphorylated proteins are known to be central molecular players in focal adhesion signaling.
“17% are known to be central molecular players in focal adhesion sig naling (Fig. 6 D and Fig. S5, A and B; Farhadi and Park, 2025; Fujita et al., 2016; Geiger, 2006; Henderson et al., 2019; Huveneers and Danen, 2009; Islam et al., 2025; Ma”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Farhadi and Park, 2025
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Self-citationProtein Kinase C-dependent Tyrosine Phosphorylation of p130 in Differentiating Neuroblastoma Cells
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Overexpression of CRKII increases migration and invasive potential in oral squamous cell carcinoma
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The Serine-rich Domain from Crk-associated Substrate (p130 ) Is a Four-helix Bundle
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CrkIII: a novel and biologically distinct member of the Crk family of adaptor proteins
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MiR-126 inhibits the invasion of gastric cancer cell in part by targeting Crk.
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Crk and CrkL present with different expression and significance in epithelial ovarian carcinoma
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A p130 Cas tyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling
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Protein phosphatase 2A interacts with the Src kinase substrate p130CAS
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BCAR1 promotes proliferation and cell growth in lung adenocarcinoma via upregulation of POLR2A
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CRKL overexpression promotes cell proliferation and inhibits apoptosis in endometrial carcinoma
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CrkI and p130Cas complex regulates the migration and invasion of prostate cancer cells
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Self-citationp130Cas/BCAR1 and p140Cap/SRCIN1 Adaptors: The Yin Yang in Breast Cancer?
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The unique function of p130Cas in regulating the bone metabolism
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Crk II silencing down-regulates IGF-IR and inhibits migration and invasion of prostate cancer cells
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Shi, L., Racedo, S. E., Diacou, A., Park, T., Zhou, B., & Morrow, B. E. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab313 · Cited by 8 · see citing works
Self-citationThe interaction of CFLAR with p130Cas promotes cell migration
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Requirement for Crk and CrkL during postnatal lens development
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Self-citationCrk and Crkl Are Required in the Endocardial Lineage for Heart Valve Development
Wu, B., Wu, B., Benkaci, S., Shi, L., Lu, P., Park, T., Morrow, B. E., Wang, Y., & Zhou, B. (2023) · Journal of the American Heart Association · doi:10.1161/jaha.123.029683 · Cited by 6 · see citing works
Self-citationCrk and CrkL are required for cell transformation by v‐ fos and v‐ ras
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Self-citationUemura, S., Wang, L., Tsuda, M., Suzuka, J., Tanikawa, S., Sugino, H., Nakamura, T., Mitsuhashi, T., Hirano, S., & Tanaka, S. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.105 · Cited by 6 · see citing works
CRK SH3N Domain Diminishes Cell Invasiveness of Non-Small Cell Lung Cancer
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Park, T., Large, N., & Curran, T. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100390 · Cited by 5 · see citing works
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Self-citationCrk/Crkl regulates early angiogenesis in mouse embryos by accelerating endothelial cell maturationPreprint
Shi, L., Song, H., Zhou, B., & Morrow, B. E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.12.548782 · Cited by 1 · see citing works
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Rac1 in gastric cancer: a molecular driver of invasion, EMT, and therapeutic resistance
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Research Progress on FAK in Neurological Diseases
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Matrix stress relaxation promotes glioblastoma cell migration in a ligand-specific manner
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Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis
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- Authors
- Farhadi, P., & Park, T.
- Affiliations
- Kermanshah University of Medical Sciences (IR)
- Children’s Mercy Research Institute, Children’s Mercy Kansas City, Kansas City, MO 64108, USA
- ORCID
- Park, Taeju
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2025-04-24
- Volume
- 26
- Issue
- 9
- Pages
- 4017
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC12071665
- OpenAlex
- W4409768903
- Cited by
- 10
- References
- 141
- Citations by year
- 2026: 8 · 2025: 2
- FWCI
- 0.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Natalie’s A.R.T. Foundation
- Masonic Cancer Alliance Partners Advisory Board grant from Children’s Mercy Hospital
- University of Kansas Cancer Center (KUCC)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
- Keywords
- p130Cas, Crk, CRKL, adaptor proteins, tumor cell migration, tumor invasion, cancer therapy targets, protein-protein interaction, anticancer drug development
- MeSH terms
- Animals, Humans, Neoplasm Invasiveness, Neoplasms, Nuclear Proteins, Signal Transduction, Adaptor Proteins, Signal Transducing, Crk-Associated Substrate Protein, Proto-Oncogene Proteins c-crk
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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