High impact information on mbo

• We have identified the first endogenous targets of the mbo nuclear import pathway in the Rel proteins Dorsal and Dif [1].
• The phenotypes of mbo mutants and mbo expression during development are cell specific, indicating that the nuclear import capacity of cells is differentially regulated [1].
• Here we describe the Drosophila gene members only (mbo) encoding a nucleoporin homologous to the mammalian Nup88 [1].
• DNup88 binds to DNup214 and DCRM1 in vitro, and both proteins become mislocalized from the nuclear rim into the nucleus of mbo mutants [2].
• We propose that a major function of DNup88 is to anchor DNup214 and CRM1 on the nuclear envelope and thereby attenuate NES-mediated nuclear export [2].

Biological context of mbo

• Nuclear import of an nuclear localization signal-enhanced green fluorescent protein (NLS-EGFP) reporter is not affected in DNup88 (members only; mbo) mutants, whereas the level of CRM1-dependent EGFP-nuclear export signal (EGFP-NES) export is increased [2].
• Our results demonstrate that distinct nuclear import events require different nucleoporins in vivo and suggest a regulatory role for mbo in signal transduction [1].

Anatomical context of mbo

• In turn, Nup88 was sufficient for targeting the complex to the nuclear pores [3].

Other interactions of mbo

• The Drosophila nucleoporin Nup88 is selectively required for nuclear accumulation of Rel proteins and full activation of the innate immune response [2].

References