PXD063151-1

PXD063151 is an original dataset announced via ProteomeXchange.

Title	Polyamines stimulate the protein synthesis of the initiation factor eIF5A2 participating in mRNA decoding distinct from eIF5A1
Description	Polyamines are present in all living organisms, and their homeostasis is closely associated with human health and disease. Further, they are small aliphatic cations that exhibit multifunctional activities through interactions with acidic substances, thereby precluding our understanding of their molecular functions in biological processes. eIF5A1 and eIF5A2 share high amino acid sequence similarity, and hypusination, using spermidine, is essential for their functions. eIF5A1 is ubiquitously expressed in all tissues and is essential for normal cell growth, whereas eIF5A2 is often expressed in human cancer tissues; however, the functional differences between eIF5A1 and eIF5A2 remain unclear. Here, we found that eIF5A2 is regulated by polyamines at the translational level and that eIF5A2, rather than eIF5A1, is important for cancer cell growth. The translational initiation of eIF5A2 mRNA was negatively regulated by miR-6514-5p at the 5ʹ-UTR, and polyamines inhibited this miRNA function, facilitating eIF5A2 synthesis. A proteomic analysis of cells with either eIF5A1 or eIF5A2 silenced showed distinct profiles. In addition, polyamines upregulated the expression of four ribosomal proteins, particularly RPS27A, RPL36A, and RPL22L1, which are associated with cancer malignancy. Our findings reveal an important role for eIF5A2, regulated by polyamines and miR-6514-5p, in cancer cell proliferation, suggesting that the interaction between eIF5A2 and ribosomes, which regulate cancer progression, is a selective target for cancer treatment.
HostingRepository	PRIDE
AnnounceDate	2025-08-25
AnnouncementXML	Submission_2025-08-24_17:31:52.843.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD063151
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Takehiro Suzuki
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2025-04-21 01:19:58	ID requested
⏵ 1	2025-08-24 17:31:53	announced

10.6019/PXD063151;

10.1016/j.jbc.2025.110453;

Suzuki M, Suzuki T, Nakano Y, Matsumoto K, Manaka H, Komeno M, Tamori S, Sato A, Dohmae N, Akimoto K, Miyazaki S, Suda T, Toida T, Kashiwagi K, Igarashi K, Higashi K, Polyamines stimulate the protein synthesis of the translation initiation factor eIF5A2, participating in mRNA decoding, distinct from eIF5A1. J Biol Chem, 301(8):110453(2025) [pubmed]

submitter keyword: polyamine, proteomics, eukaryotic initiation factor 5A (eIF5A), cell proliferation, spermidine

Naoshi Dohmae
contact affiliation	Biomolecular characterization unit, Center for Sustainable Resource Science, RIKEN
contact email	dohmae@riken.jp
lab head
Takehiro Suzuki
contact affiliation	RIKEN Center for Sustainable Resource Science
contact email	takehirosuzuki@riken.jp
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/08/PXD063151

PRIDE project URI

• PRIDE
  1. PXD063151
     1. Label: PRIDE project
     2. Name: Polyamines stimulate the protein synthesis of the initiation factor eIF5A2 participating in mRNA decoding distinct from eIF5A1