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Study describes how adhesion molecules rearrange their interactions to exit cell junctions.

People & Ideas

Cossart studies how Listeria monocytogenes manipulates the biology of its host cells.



ER stress induces expression of miR-708, which suppresses the production of rhodopsin to prevent ER overloading in retinal epithelial cells.

PGL proteins act as scaffolds that recruit RNPs during C. elegans germ granule formation.

Like the nuclear pore complex, FG repeat–containing P-granule proteins interact to help establish a size-exclusion barrier.

The use of new candidate markers for yeast quiescence reveals that quiescence entry and exit primarily rely on cellular metabolic status and can be uncoupled from the cell cycle.

Kinastrin is identified as a major interacting partner for astrin in mitotic cells, and is required for astrin targeting to microtubule plus ends.

In addition to its function as an initiator of DNA replication, vertebrate Orc6 is also required for the final step of cytokinesis.


Association of Akt with phosphatidylserine enhances binding to PIP3, inducing conformational changes in Akt that promote its phosphorylation-mediated activation.

Centrosomal localization of kinase-active CK1δ is required for neurite outgrowth in response to Wnt-3a.

Mapping of fission yeast precursor node interaction modules and assembly reveals important steps in contractile ring assembly.

Eight proteins, defects in which are associated with Meckel-Gruber syndrome and nephronophthisis ciliopathies, work together as two functional modules at the transition zone to establish basal body/transition zone connections with the membrane and barricade entry of non-ciliary components into this organelle.

Pah1p promotes lipid droplet assembly independent of its role in triacylglycerol synthesis.

Fzd9, induced upon osteoblast differentiation, is required for bone matrix mineralization in primary osteoblasts.

Intercellular traction forces or lateral alignment of cadherin molecules can influence adherens junction dynamics by altering the cadherin dimerization interface.

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