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Cover Image
Cover Image
On the cover
A HeLa cell plated onto an L-shaped, fibronectin-coated micropattern forms prominent retraction fibers containing F-actin (green) that help to orient the mitotic spindle. Machicoane et al. reveal that spindle orientation is promoted by the SLK kinase–dependent activation of the actin-binding ezrin/radixin/moesin (ERM) family.
Image © 2014 Machicoane et al.
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In This Issue
In Focus
A different angle on cell division
Study shows how actin-binding proteins help tilt the mitotic spindle.
People & Ideas
Fernando Martín-Belmonte: Epithelia embrace the space
Martín-Belmonte studies epithelial morphogenesis in 3D culture and in zebrafish.
Review
Report
HDAC4 integrates PTH and sympathetic signaling in osteoblasts
During osteoclast differentiation, two extracellular cues that induce cAMP production both converge on HDAC4 and induce Rankl expression but do so using distinct signaling pathways.
Mps1 phosphorylation of condensin II controls chromosome condensation at the onset of mitosis
Mps1 is necessary for proper condensin II loading onto chromatin and subsequent chromosome condensation during mitosis.
SLK-dependent activation of ERMs controls LGN–NuMA localization and spindle orientation
ERM activation by SLK kinase promotes polarized association at the mitotic cortex of LGN and NuMA, a necessary step in proper spindle orientation.
A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans
The ZP251–149 domain is necessary for human and mouse gamete recognition on the surface of the zona pellucida and for mouse fertility.
Article
SIVA1 directs the E3 ubiquitin ligase RAD18 for PCNA monoubiquitination
The RAD18 E3 ligase requires SIVA1 as an accessory protein for binding to its substrate PCNA during translesion DNA synthesis.
The Cavβ1a subunit regulates gene expression and suppresses myogenin in muscle progenitor cells
Cavβ1a acts as a voltage-gated calcium channel-independent regulator of gene expression in muscle progenitor cells and is required for their normal expansion during myogenic development.
Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins
Intramembrane proteolytic cleavage by signal peptide peptidase is required for the turnover of some ER-resident, tail-anchored membrane proteins.
