Drosophila integrin adhesion complexes are essential for hemocyte migration in vivo.

Cell migration is an important biological process which has been intensively studied in the past decades. Numerous techniques, mainly involving two-dimensional cell culture systems, have contributed to dissecting the essential mechanisms underlying this process. However, the development of three-dimensional cell culture and in vivo systems has shown some differences with what was previously believed to be well-established cell migration mechanisms, suggesting that two-dimensional cell motility would be a poor predictor of in vivo behaviour.

DRhoGEF2 regulates cellular tension and cell pulsations in the Amnioserosa during Drosophila dorsal closure.

Coordination of apical constriction in epithelial sheets is a fundamental process during embryogenesis. Here, we show that DRhoGEF2 is a key regulator of apical pulsation and constriction of amnioserosal cells during Drosophila dorsal closure. Amnioserosal cells mutant for DRhoGEF2 exhibit a consistent decrease in amnioserosa pulsations whereas overexpression of DRhoGEF2 in this tissue leads to an increase in the contraction time of pulsations.

Drosophila hemocyte migration: an in vivo assay for directional cell migration.

This protocol describes an in vivo assay for random and directed hemocyte migration in Drosophila. Drosophila is becoming an increasingly powerful model system for in vivo cell migration analysis, combining unique genetic tools with translucency of the embryo and pupa, which allows direct imaging and traceability of different cell types. In the assay we present here, we make use of the hemocyte response to epithelium wounding to experimentally induce a transition from random to directed migration.

Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome.

The 26 S proteasome is a large proteolytic machine, which degrades most intracellular proteins. We found that thioredoxin, Txnl1/TRP32, binds to Rpn11, a subunit of the regulatory complex of the human 26 S proteasome. Txnl1 is abundant, metabolically stable, and widely expressed and is present in the cytoplasm and nucleus.