Abstract
Unclouding (some of) the moonlighting functions of eEF1A2: Spontaneous mutations in the EEF1A2 gene are increasingly being recognized as a source of epilepsy and severe neurological disabilities in children. The crystal structure of eEF1A2 protein purified from rabbit skeletal muscle reveals the spatial locations of the side-chain carboxylates of Glu301 and Glu374, to which phosphatidylethanolamine is uniquely attached via an amide bond, thereby defining the anchoring points of an eEF1A2 dimer to cellular membranes. In this new light, the role of eEF1A2 as an ancient, multifaceted, and articulated G protein at the crossroads of autophagy, oncogenesis, and viral replication appears very distant from the “canonical” one of delivering aminoacyl-tRNAs to the ribosome that has dominated the scene and much of the thinking for many decades. More information can be found in the full paper by J. A. Hermoso, F. Gago, et al.
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