CacyBP/SIP binds ERK1/2 and affects transcriptional activity of Elk-1

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• 作者：Ewa Kilanczyk ; Slawomir Filipek ; Beata Jastrzebska ; Anna Filipek
• 关键词：CacyBP/SIP ; Elk-1 ; ERK1/2 ; NB2a cells ; S100A6
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2009
• 出版时间：27 February 2009
• 年：2009
• 卷：380
• 期：1
• 页码：54-59
• 全文大小：536 K

文摘

In this work we showed for the first time that mouse CacyBP/SIP interacts with extracellular signal regulated kinases 1 and 2 (ERK1/2). We also established that a calcium binding protein, S100A6, competes for this interaction. Moreover, the E217K mutant of CacyBP/SIP does not bind significantly to ERK1/2 although it retains the ability to interact with S100A6. Molecular modeling shows that the E217K mutation in the 189–219 CacyBP/SIP fragment markedly changes its electrostatic potential, suggesting that the binding with ERK1/2 might have an electrostatic character. We also demonstrate that CacyBP/SIP-ERK1/2 interaction inhibits phosphorylation of the Elk-1 transcription factor in vitro and in the nuclear fraction of NB2a cells. Altogether, our data suggest that the binding of CacyBP/SIP with ERK1/2 might regulate Elk-1 phosphorylation/transcriptional activity and that S100A6 might further modulate this effect via Ca²⁺-dependent interaction with CacyBP/SIP and competition with ERK1/2.