K-Ras Lys-42 is crucial for its signaling, cell migration, and invasion
Open accessAbstract
Ras proteins participate in multiple signal cascades, regulating crucial cellular processes, including cell survival, proliferation, and differentiation. We have previously reported that Ras proteins are modified by sumoylation and that Lys-42 plays an important role in mediating the modification. In the current study, we further investigated the role of Lys-42 in regulating cellular activities of K-Ras. Inducible expression of K-Ras V12 led to the activation of downstream components, including c-RAF, MEK1, and extracellular signal–regulated kinases (ERKs), whereas expression of K-Ras V12/R42 mutant compromised the activation of the RAF/MEK/ERK signaling axis. Expression of K-Ras V12/R42 also led to reduced phosphorylation of several other protein kinases, including c-Jun N-terminal kinase (JNK), Chk2, and focal adhesion kinase (FAK). Significantly, K-Ras V12/R42 expression inhibited cellular migration and invasion in vitro in multiple cell lines, including transformed pancreatic cells. Given that K-Ras plays a crucial role in mediating oncogenesis in the pancreas, we treated transformed pancreatic cells of both BxPC-3 and MiaPaCa-2 with 2-D08, a small ubiquitin-like modifier (SUMO) E2 inhibitor. Treatment with the compound inhibited cell migration in a concentration-dependent manner, which was correlated with a reduced level of K-Ras sumoylation. Moreover, 2-D08 suppressed expression of ZEB1 (a mesenchymal cell marker) with concomitant induction of ZO-1 (an epithelial cell marker). Combined, our studies strongly suggest that posttranslational modification(s), including sumoylation mediated by Lys-42, plays a crucial role in K-Ras activities in vivo .
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Overexpression of wild-type KRAS significantly stimulated cell migration, which is further promoted by KRAS (G12V).
“The overexpression of wild-type KRAS significantly stimulated cell migration, which is further promoted by KRAS (G12V) [54, 55].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [55]
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- Authors
- Choi, B. H., Philips, M. R., Chen, Y., Lu, L., & Dai, W.
- Affiliations
- NYU Langone Health (US)
- City Of Hope National Medical Center (US)
- University of California, Los Angeles (US)
- Corresponding author
- Dai, Wei
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2018-11
- Volume
- 293
- Issue
- 45
- Pages
- 17574-17581
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6231119
- OpenAlex
- W2890800456
- Cited by
- 42
- References
- 30
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 6 · 2023: 4 · 2022: 7 · 2021: 12 · 2020: 5 · 2019: 1
- FWCI
- 1.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Environmental Health Sciences (NIEHS) (ES000260)
- HHS | NIH | National Cancer Institute (NCI) (CA216987)
- 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 › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- KRAS, SUMOylation, MAPK/ERK pathway, cell migration, cell invasion, pancreatic cancer, ZEB1, ZO-1, epithelial-mesenchymal transition, post-translational modification, carcinogenesis
- MeSH terms
- Zinc Finger E-box-Binding Homeobox 1, Animals, Cell Movement, Humans, Neoplasm Invasiveness, Proto-Oncogene Proteins p21(ras), MAP Kinase Signaling System, NIH 3T3 Cells, Ubiquitin-Conjugating Enzymes, Flavones, Extracellular Signal-Regulated MAP Kinases, Mice, Focal Adhesion Kinase 1, HEK293 Cells, Sumoylation, MCF-7 Cells, Zonula Occludens-1 Protein, Checkpoint Kinase 2
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