YIPFα1A expression is regulated by multilayered molecular mechanisms
##article.authors##
- Tokio Takaji Division of Life Sciences, Graduate School of Kyoto Sangyo University, CRIA, Kyoto University
- Yurika Nakanishi Division of Life Sciences, Graduate School of Kyoto Sangyo University
-
Nobuhiro Nakamura
Division of Life Sciences, Graduate School of Kyoto Sangyo University
https://orcid.org/0000-0002-8836-6714
https://researchmap.jp/nnosaru3
DOI:
https://doi.org/10.51094/jxiv.1511Keywords:
Golgi, complex formation, mRNA stability, codon adaptation index, 3′ untranslated regionAbstract
YIPF is a family of five-span transmembrane proteins primarily localized at the Golgi apparatus. A YIPF α-subunit associates with a specific β-subunit partner to form a dimer, and the dimers further assemble into higher-order oligomers. The expression of an α-subunit partner is necessary for the efficient expression of its β-subunit partner. Curiously, conventional exogenous expression of α-subunits has proven extremely difficult, preventing further analysis of the YIPF complexes. To address this issue, the genetic information of YIPF was closely examined to determine why the exogenous expression of the YIPF α-subunits is inhibited. We identified two common features among YIPFs with poor exogenous expression: (1) the coding sequences of the YIPF α-subunits are enriched with rare codons, and (2) their mRNAs possess extended 3′ untranslated regions (UTRs). Our experimental evaluation of these features, focusing on YIPFα1A, revealed that both significantly influence YIPFα1A protein expression. First, the enrichment of rare codons markedly reduced YIPFα1A expression notably at the mRNA level. Second, the 3′ UTR of YIPFα1A was found to enhance its expression at the mRNA level. The deletion analysis revealed that the proximal region of the 3′ UTR, adjacent to the coding sequence, plays a key role in increasing mRNA abundance.
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Published: 2025-09-09 01:09:22 UTC
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Tokio Takaji
Yurika Nakanishi
Nobuhiro Nakamura
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