LGG-1/GABARAP lipidation is not required for autophagy and development in .

The ubiquitin-like proteins Atg8/LC3/GABARAP are required for multiple steps of autophagy, such as initiation, cargo recognition and engulfment, vesicle closure and degradation. Most of LC3/GABARAP functions are considered dependent on their post-translational modifications and their association with the autophagosome membrane through a conjugation to a lipid, the phosphatidyl-ethanolamine. Contrarily to mammals, possesses single homologs of LC3 and GABARAP families, named LGG-2 and LGG-1.

Three members of the yeast N-BAR proteins family form heterogeneous lattices in vivo and interact differentially with two RabGAP proteins.

The yeast N-BAR (Bin/Amphiphysin/Rvs167) protein Rvs167 is recruited by the Rab GTPase Activating Proteins (RabGAP) Gyp5 and Gyl1 to the tip of small buds to act in exocytosis. Investigating other N-BAR proteins involved in Gyp5/Gyl1/Rvs167 complexes, we found that Rvs161, an Rvs167 paralog, is absent from the complexes formed at the tip of small buds. Immunoprecipitation and Bimolecular Fluorescence Complementation (BiFC) analysis show that both Rvs167 and Rvs161 interact in vivo with Gvp36, an N-BAR protein.

Linking local retention, self-recruitment, and persistence in marine metapopulations.

Three indices of larval retention have been used in the literature to assess the tendency for self-maintenance of local marine populations: local retention (LR), self-recruitment (SR), and relative local retention (RLR). Only one of these, LR, defined as the ratio of locally produced settlement to local egg production, has a clear relationship to self-persistence of individual sites. However, SR, the ratio of locally produced settlement to settlement of all origins at a site, is generally easier to measure experimentally.

The recruitment of p47(phox) and Rac2G12V at the phagosome is transient and phosphatidylserine dependent.

Background Information: During phagocytosis, neutrophils internalise pathogens in a phagosome and produce reactive oxygen species (ROS) by the NADPH oxidase to kill the pathogen. The cytosolic NADPH oxidase subunits p40(phox), p47(phox), p67(phox) and Rac2 translocate to the phagosomal membrane to participate in enzyme activation. The kinetics of this recruitment and the underlying signalling pathways are only partially understood.