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In This Issue

In Focus

Study visualizes Alzheimer's disease–related peptides forming toxic calcium channels in the plasma membrane.

People & Ideas

Geiger researches the composition and function of cell adhesions.


Host–pathogen interactions


ATM and ATR display distinct activities in meiotic DSB repair, such that ATM functions in DNA damage repair and negative feedback control over programmed double strand breaks, whereas ATR is required for checkpoint activity.

The scaffolding protein Canoe regulates spindle orientation by binding to RanGTP and recruiting RanGTP and Mud to the cell cortex.

CIIA mediates the TGF-β–induced activation of SOS1–Rac1 signaling and cell migration.


A number of different genetic backgrounds and growth conditions bypass DNA replication defects caused by the absence of yeast Hsk1 kinase, demonstrating the plasticity of the eukaryotic DNA replication program.

PKA and CaM kinase II both target the histone deacetylase HDAC4 such that the former antagonizes MEF2 activity and the latter promotes it.

Expression of the essential EMT inducer Snail1 is inhibited by miR-34 through a p53-dependent regulatory pathway.

In response to amino acid availability, the class III PI-3-kinase hVps34 activates the phospholipase PLD and mTORC1 signaling to regulate mammalian cell size.

Chk1 phosphorylates Aurora B to promote its full activation during mitotic prometaphase.

Insertion into and release of the cytoplasmic domain of the Schizosaccharomyces pombe spindle pole body from a nuclear envelope fenestra during mitosis requires Brr6.

When fission yeast express mutant cofilin that is inefficient at actin filament severing, cytokinetic contractile ring formation is severely impaired, but ring contraction proceeds efficiently.

Talin recruits and activates focal adhesion proteins required for cell cycle progression.

High-resolution imaging of calcium influx reveals that the Aβ peptides implicated in Alzheimer’s disease form highly toxic Ca2+-permeable pores.

Clathrin assembles at bacterial adhesion sites and its phosphorylation is required for actin recruitment during bacterial infection.

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