Colonization and development of Oribatida mite communities (Acari: Oribatida) in the forest reclaimed limestone mine dumps

In order to study the colonization and development of moss mites (Oribatida) communities in a Scots pine forest of a reclaimed limestone mine dump in Northern Poland, 3 plots from the dump were chosen. The selected plots differed in age, 5 years old, 35 and 50 years old. From a total of 30 samples 499 mites (Acari) were extracted in Tullgren funnel from which 262 were Oribatida. Abundance (N) was analyzed in all mites and after determining the species of both, juvenile and adult stages of oribatids, the following indices were analyzed: Abundance (N), Dominance (D), Species diversity (S), Species richness (s) and Shannon’s diversity index (H). Regarding to the results obtained; oribatid mites were dominant with the highest abundance in all assemblages (Plot 1: 139 Oribatida /299 Acari. Plot 2: 40/55 and Plot 3: 83/145). Tectocepheus velatus showed a very high dominance (45,99%) in plot 1; the highest value for Shannon’s diversity index belonged to plot 3. On the other hand, juvenile’s percentage was significantly higher than adult’s percentage, especially at plot 2 (95,02%). These results made us to conclude that the high abundance of oribatids in the youngest forest is due to T. velatus’s high abundance and that plot 3 is the best habitat for mites. Finally, the high occurrence of juvenile stages requires keeping on studying the area.

Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1

Dynamin-Related Protein 1 (Drp1), a large GTPase of the dynamin superfamily, is required for mitochondrial fission in healthy and apoptotic cells. Drp1 activation is a complex process that involves translocation from the cytosol to the mitochondrial outer membrane (MOM) and assembly into rings/spirals at the MOM, leading to membrane constriction/division. Similar to dynamins, Drp1 contains GTPase (G), bundle signaling element (BSE) and stalk domains. However, instead of the lipid-interacting Pleckstrin Homology (PH) domain present in the dynamins, Drp1 contains the so-called B insert or variable domain that has been suggested to play an important role in Drp1 regulation. Different proteins have been implicated in Drp1 recruitment to the MOM, although how MOM-localized Drp1 acquires its fully functional status remains poorly understood. We found that Drp1 can interact with pure lipid bilayers enriched in the mitochondrion-specific phospholipid cardiolipin (CL). Building on our previous study, we now explore the specificity and functional consequences of this interaction. We show that a four lysine module located within the B insert of Drp1 interacts preferentially with CL over other anionic lipids. This interaction dramatically enhances Drp1 oligomerization and assembly-stimulated GTP hydrolysis. Our results add significantly to a growing body of evidence indicating that CL is an important regulator of many essential mitochondrial functions.