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A more recent version of this article appeared on March 1, 2004
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Submitted on September 3, 2003
Revised on November 12, 2003
Accepted on November 18, 2003
1 Dipartimento di Sanità Pubblica e Biologia Cellulare, University of Rome "Tor Vergata"
2 Istituto di Endocrinologia e Oncologia Sperimentale del CNR c/o Dipartimento di Biologia e Patologia Cellulare e Molecolare, University of Naples "Federico II"
3 Dipartimento di Medicina Sperimentale, II University of Naples
4 Dipartimento di Sanità Pubblica e Biologia Cellulare, Università di Roma "Tor Vergata", Via Montpellier 1 00133, Rome, ITALY
* Corresponding author. E-mail address: claudio.sette{at}uniroma2.it.
The MAPK pathway is required for maintaining the chromatin condensed during the two meiotic divisions and to avoid a second round of DNA duplication. However, molecular targets of the MAPK pathway on chromatin have not yet been identified. Here we show that the architectural chromatin protein HMGA2 is highly expressed in male meiotic cells. Furthermore, Nek2, a serine-threonine kinase activated by the MAPK pathway in mouse pachytene spermatocytes, directly interacts with HMGA2 in vitro and in mouse spermatocytes. The interaction does not depend on the activity of Nek2 and appears constitutive. On progression from pachytene to metaphase, Nek2 is activated and HMGA2 is phosphorylated in a MAPK-dependent manner. We also show that Nek2 phosphorylates in vitro HMGA2 and that this phosphorylation decreases the affinity of HMGA2 for DNA and might favor its release from the chromatin. Indeed, we find that most HMGA2 associates with chromatin in mouse pachytene spermatocytes, whereas it is excluded from the chromatin upon the G2/M progression. Since hmga2-/- mice are sterile and show a dramatic impairment of spermatogenesis, it is possible that the functional interaction between HMGA2 and Nek2 plays a crucial role in the correct process of chromatin condensation in meiosis.
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