Pav-KLP is the Drosophila member of the MKLP1 family essential for cytokinesis. In the syncytial blastoderm embryo, GFP-Pav-KLP cyclically associates with astral, spindle, and midzone microtubules and also to actomyosin pseudocleavage furrows. As the embryo cellularizes, GFP-Pav-KLP also localizes to the leading edge of the furrows that form cells. In mononucleate cells, nuclear localization of GFP-Pav-KLP is mediated through NLS elements in its C-terminal domain. Mutants in these elements that delocalize Pav-KLP to the cytoplasm in interphase do not affect cell division. In mitotic cells, one population of wild-type GFP-Pav-KLP associates with the spindle and concentrates in the midzone at anaphase B. A second is at the cell cortex on mitotic entry and later concentrates in the region of the cleavage furrow. An ATP binding mutant does not localize to the cortex and spindle midzone but accumulates on spindle pole microtubules to which actin is recruited. This leads either to failure of the cleavage furrow to form or later defects in which daughter cells remain connected by a microtubule bridge. Together, this suggests Pav-KLP transports elements of the actomyosin cytoskeleton to plus ends of astral microtubules in the equatorial region of the cell to permit cleavage ring formation.

ABSTRACT. Several G proteins of the Rho family have been shown to be required for cytokinesis. The activity of these proteins is regulated by GTP exchange factors (GEFs), which stimulate GDP/GTP exchange, and by GTPase activating proteins (GAPs), which suppress activity by stimulating the intrinsic GTPase activity. The role of Rho family members during cytokinesis is likely to be determined by their spatial and temporal interactions with these factors. Here we focus on the role of the pebble (pbl) gene of Drosophila melanogaster, a RhoGEF that is required for cytokinesis. We summarise the evidence that the primary target of PBL is Rho1 and describe genetic approaches to elucidating the function of PBL and identifying other components of the PBL-activated Rho signalling pathway.Key words: cytokinesis/G proteins/Rho/Drosophila/actin cytoskeleton Small G proteins (GTPases) of the Ras superfamily play key roles in a variety of intracellular signalling pathways within eukaryotic cells. These signalling pathways are employed in many aspects of cellular function, including regulation of the actin cytoskeleton. It is therefore no surprise that members of one subclass, the Rho family of small G proteins, have been implicated in cytokinesis. In this paper, we summarise the evidence in support of a role for Rho family proteins in cytokinesis, and discuss our recent investigations into their regulation by the Rho GTP exchange factor (RhoGEF) encoded by the pebble (pbl) gene of Drosophila melanogaster.