Degradation and asymmetric inheritance during cell division of a core pluripotency regulator contributes to lineage commitment in the early Xenopus embryo.

During meiosis, budding yeast use a checkpoint involving the protein Mec1 to prevent the formation of double-strand breaks in DNA that has not completed replication.

Phosphoproteomics identifies β-arrestin 2 phosphorylation at Thr383 by MEK as a key step of GPCR-induced Erk½ activation, thus providing new insight into the molecular mechanism underlying β-arrestin-dependent GPCR-operated signaling.

Retrograde signaling activates the Rad53 checkpoint kinase independently of the canonical DNA replication stress response.

Genetic and biochemical analyses uncover a dichotomy of ERK pathway functions in osteoblasts, whereby ERK activation promotes the early differentiation of osteoblast precursors, but inhibits the subsequent differentiation of committed osteoblasts via mTOR-mediated regulation of mitochondrial function and SGK1.

Two cell-penetrating peptides that inhibit Ras-ERK signalling and a potent clinically relevant MEK inhibitor block cocaine conditioned place preference and accelerate extinction of cocaine self-administration upon a single administration in mice.

Aberrant ERK/MAPK signaling in cortical pyramidal neurons leads to selective disruption of layer 5 circuit development and generalized changes in neuronal excitability.

The conversion of the ends of a double-strand break from double-stranded to single-stranded DNA, which is necessary to initiate homologous recombination, is responsible for loss of transcription and RNA polymerase occupancy around the double-strand break in Saccharomyces cerevisiae.

Low-dose treatment targeting multiple pathways of a pro-metastatic signaling network reduces the metastatic output of heterogeneous tumors while minimizing compensatory network activation.