RNF135 promotes cell proliferation and autophagy in lung adenocarcinoma by promoting the phosphorylation of ULK1

Allergol Immunopathol (Madr). 2024 Mar 1;52(2):3-9. doi: 10.15586/aei.v52i2.1048. eCollection 2024.

Abstract

Objective: To detect the expression of RING finger protein 135 (RNF135) in lung adenocarcinoma tissues and explore its role in the progression of lung adenocarcinoma.

Methods: Bioinformation analysis, quantitative polymerase chain reaction, and immunoblotting technique discovered the expression of RNF135 in lung adenocarcinoma tissues. Cell counting kit-8 and colony formation, immunostaining, and immunoblot assays examined the effects of RNF135 on cell growth and autophagy. Co-immunoprecipitation (Co-IP), immunostaining, and immuoblotting were conducted to confirm the mechanism.

Results: RNF135 was highly expressed in lung adenocarcinoma. In addition, RNF135 promoted lung adenocarcinoma cell growth. Further, data confirmed that RNF135 promoted autophagy in lung adenocarcinoma cells. Mechanically, RNF135 directly interacted with Unc-51-like autophagy activating kinase 1 (ULK1) to promote its phosphorylation level.

Conclusion: RNF135 promoted cell growth and autophagy in lung adenocarcinoma by promoting the phosphorylation of ULK1.

Keywords: Autophagy; Lung Adenocarcinoma; Phosphorylation; Rnf135; Ulk1.

MeSH terms

  • Adenocarcinoma of Lung*
  • Autophagy
  • Autophagy-Related Protein-1 Homolog / metabolism
  • Cell Proliferation
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Intracellular Signaling Peptides and Proteins / pharmacology
  • Lung Neoplasms* / pathology
  • Phosphorylation
  • Ubiquitin-Protein Ligases* / genetics
  • Ubiquitin-Protein Ligases* / metabolism
  • Ubiquitin-Protein Ligases* / pharmacology

Substances

  • Autophagy-Related Protein-1 Homolog
  • Intracellular Signaling Peptides and Proteins
  • RNF135 protein, human
  • Ubiquitin-Protein Ligases
  • ULK1 protein, human