eIF4A1 is a promising new therapeutic target in ER-negative breast cancer

Given the role of protein synthesis control in gene expression regulation, it is unsurprising that aberrant control of translation is associated with tumorigenesis.² This can occur by enhanced signalling through to translation, releasing protein required for eIF4F complex formation (e.g., eIF4E) from their negative regulators.¹ Several chemotherapeutic agents target pathways that activate protein synthesis are in development (reviewed in Blagden and Willis³) and in particular there has been much interest in inhibitors of the PI3K/mTOR pathway, several of which are in clinical use as cancer treatments.

A number of recent studies have also shown that the helicase component of the eIF4F complex, eIF4A1 and the proteins that are known to modulate its function, including eIF4B, eIF4H, PDCD4 and eIF4E,⁴ have a crucial role in the progression and development of tumours.

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