Desmoplakin assembly dynamics in four dimensions: multiple phases differentially regulated by intermediate filaments and actin.

The intermediate filament (IF)-binding protein desmoplakin (DP) is essential for desmosome function and tissue integrity, but its role in junction assembly is poorly understood. Using time-lapse imaging, we show that cell-cell contact triggers three temporally overlapping phases of DP-GFP dynamics: (1) the de novo appearance of punctate fluorescence at new contact zones after as little as 3 min; (2) the coalescence of DP and the armadillo protein plakophilin 2 into discrete cytoplasmic particles after as little as 15 min; and (3) the cytochalasin-sensitive translocation of cytoplasmic particles to maturing borders, with kinetics ranging from 0.002 to 0.

Terminating Wnt signals: a novel nuclear export mechanism targets activated (beta)-catenin.

Nuclear targeting of beta-catenin is an obligatory step in Wnt signal transduction, but the factors that control import and export remain to be clarified. In this issue, Hendriksen et al. (p.

Heat-induced oligomerization of gp96 occurs via a site distinct from substrate binding and is regulated by ATP.

Gp96 (GRP94) is a dimeric glycoprotein and is the endoplasmic reticulum representative of the hsp90 family of molecular chaperones. In addition to the protein substrates it chaperones, gp96 binds weakly to both peptides and ATP, and has been shown to self-assemble into discrete oligomers upon heat shock at 50 degrees C, although physiological roles for these phenomena have not been well established. Our studies indicate that gp96 homooligomerizes irreversibly in vitro at temperatures as low as 42 degrees C and could involve pre-dissociation of dimers to monomers.