PUF60 is a Critical Regulator of PKM Splicing During Myogenesis.

Authors

So Masaki, Takayuki Nojima, Takako Oshiro-Ideue, Asami Suenaga, Akihide Takeuchi, Isao Kii, Kenji Suzuki, Satoshi Tanaka, Masatoshi Hagiwara, Naoyuki Kataoka

Published in

Molecular and cellular biology. Pages 1-16. Jul 14, 2026. Epub Jul 14, 2026.

Abstract

Pyruvate kinase M (PKM) catalyzes the conversion of phosphoenolpyruvate to pyruvate in glycolysis and exists as two splice isoforms, PKM1 and PKM2, generated from alternative splicing of mutually exclusive exons 9 or 10, respectively. The expression balance between PKM1 and PKM2 is tightly regulated in a cell-type-specific manner. PKM1 is predominantly expressed in tissues such as skeletal muscle, heart, and brain, whereas PKM2 is prevalent in most other tissues and various cancer cells. Despite its importance, the trans-acting factors promoting exon 9 selection in a tissue-specific context remain largely unknown. Here, using a multi-color splicing reporter system for cell-based cDNA screening, we identified PUF60 as a novel trans-acting factor that promotes PKM1-type splicing. We also demonstrated that PUF60 induction and the resulting splicing switch are essential for myotube formation during C2C12 differentiation. This study establishes PUF60 as a critical regulator of muscle-specific splicing and provides new insights into the fundamental mechanisms governing skeletal muscle differentiation.

PMID:
42446402
Bibliographic data and abstract were imported from PubMed on 14 Jul 2026.

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