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Finding biologically relevant targets is a prerequisite for understanding the function of any trans regulator of gene expression, but this can be particularly challenging with microRNAs (miRNAs). A study in this issue addresses the problem by identifying a novel mode of miRNA target recognition.
A complex of PUF (named after founding members Pumilio and Fem-3 binding factor) and Argonaute proteins can stall translation elongation on bound mRNAs by interacting with eEF1A and inhibiting its GTPase activity.
The Cbl family of RING finger ubiquitin ligases regulates signaling in many systems. Two new studies provide a structural basis for how phosphorylation of a specific tyrosine in the Cbl proteins enhances their ubiquitin ligase activity, giving insight into how ubiquitination by Cbl proteins is restricted to specific substrates.
The proteins that 'pump' neurotransmitters into neurons, clearing the synapse after a nerve impulse, are central players in coherent brain function and are targets of many psychotropic drugs. Two groups now endeavor to resolve a fundamental controversy about how these proteins work. The results shed new light on the controversy but do not end it.
Structural studies of the epidermal growth factor receptor (EGFR) have advanced greatly in recent years, but they have used a 'divide-and-conquer' approach for independent study of the intracellular and extracellular regions. Several recent papers provide important new perspectives on 'undivided' EGFR and describe the initial steps in reconstructing signaling behavior of the intact receptor.
Oncogene-induced replication stress and DNA damage are among the hallmarks of cancer. A recent study explores how different levels of replication stress affect animal development and tumorigenesis, and how targeting of the replication stress–signaling pathway of ATR and Chk1 kinases can be exploited for selective killing of cancer cells.
