2. Academic Validation
  3. βTrCP1 promotes SLC35F2 protein ubiquitination and inhibits cancer progression in HeLa cells

βTrCP1 promotes SLC35F2 protein ubiquitination and inhibits cancer progression in HeLa cells

  • Biochem Biophys Res Commun. 2023 Sep 30:682:27-38. doi: 10.1016/j.bbrc.2023.09.095.
Jencia Carminha Colaco 1,  Arun Pandian Chandrasekaran 1,  Janardhan Keshav Karapurkar 1,  Girish Birappa 1,  Sripriya Rajkumar 1,  D A Ayush Gowda 1,  Bharathi Suresh 1,  Junwon Lee 2,  Vijai Singh 3,  Seok-Ho Hong 4,  Kye-Seong Kim 5,  Suresh Ramakrishna 6
Affiliations

Affiliations

  • 1 Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, 04763, South Korea.
  • 2 Institute of Vision Research, Department of Ophthalmology, Gangnam Severance Hospital, Yonsei University College of Medicine, Eonjuro 211, Gangnam-Gu, Seoul, 06273, South Korea.
  • 3 Department of Biosciences, School of Science, Indrashil University, Rajpur, Mehsana, 382715, Gujarat, India.
  • 4 Department of Internal Medicine, School of Medicine, Kangwon National University, Chuncheon, South Korea. Electronic address: shhong@kangwon.ac.kr.
  • 5 Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, 04763, South Korea; College of Medicine, Hanyang University, Seoul, 04763, South Korea. Electronic address: ks66kim@hanyang.ac.kr.
  • 6 Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, 04763, South Korea; College of Medicine, Hanyang University, Seoul, 04763, South Korea. Electronic address: suresh.ramakris@gmail.com.
PMID: 37801987 DOI: 10.1016/j.bbrc.2023.09.095
Abstract

The solute carrier family 35 F2 (SLC35F2) belongs to membrane-bound carrier proteins that are associated with multiple cancers. The main factor that determines Cancer progression is the expression level of SLC35F2. Thus, identifying the E3 Ligase that controls SLC35F2 protein abundance in Cancer cells is critical. Here, we identified βTrCP1 interacting with and reducing the SLC35F2 protein level. βTrCP1 signals SLC35F2 protein ubiquitination and reduces SLC35F2 protein half-life. The mRNA expression pattern between βTrCP1 and SLC35F2 across a panel of Cancer cell lines showed a negative correlation. Additionally, the depletion of βTrCP1 accumulated SLC35F2 protein and promoted SLC35F2-mediated cell growth, migration, invasion, and colony formation ability in HeLa cells. Overall, we demonstrate that βTrCP1 acts as a tumor suppressor by controlling SLC35F2 protein abundance in Cancer cells. The depletion of βTrCP1 promotes SLC35F2-mediated carcinogenesis. Thus, we envision that βTrCP1 may be a potential target for Cancer therapeutics.

Keywords

Post-translational modifications; Protein destabilization; Protein ubiquitination; Proteolysis; Wound healing.

Figures
Products