ERK-dependent protein phosphorylation in KRAS-mutant cancer: a mix of the expected and surprising

Kevin Huang; Yubao Wang; Thomas M Roberts

doi:10.1016/j.tibs.2024.10.011

ERK-dependent protein phosphorylation in KRAS-mutant cancer: a mix of the expected and surprising

Trends Biochem Sci. 2025 Jan;50(1):6-8. doi: 10.1016/j.tibs.2024.10.011. Epub 2024 Nov 16.

Authors

Kevin Huang¹, Yubao Wang², Thomas M Roberts³

Affiliations

¹ Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
² Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA. Electronic address: yubao_wang@dfci.harvard.edu.
³ Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA. Electronic address: thomas_roberts@dfci.harvard.edu.

PMID: 39551665
PMCID: PMC11698634 (available on 2026-01-01)
DOI: 10.1016/j.tibs.2024.10.011

Abstract

Recently developed KRAS inhibitors have delivered clinical benefits but their antitumor efficacy remains limited. A recent study by Klomp et al. reports an unprecedentedly comprehensive profiling of protein phosphorylation dependent on the KRAS pathway and generates new insights and directions to improve the efficacy of KRAS-targeted therapies.

Keywords: ERK; KRAS; MEK; phosphorylation.

MeSH terms

Extracellular Signal-Regulated MAP Kinases / metabolism
Humans
Mutation*
Neoplasms* / drug therapy
Neoplasms* / genetics
Neoplasms* / metabolism
Phosphorylation
Proto-Oncogene Proteins p21(ras)* / genetics
Proto-Oncogene Proteins p21(ras)* / metabolism

Substances

Proto-Oncogene Proteins p21(ras)
KRAS protein, human
Extracellular Signal-Regulated MAP Kinases

Grants and funding

R35 CA231945/CA/NCI NIH HHS/United States