In this paper, we analyze and compare nest composition and architecture as well as worker relatedness in three related species of slave‐making ants: Rossomyrmex anatolicus, R. minuchae, and R. quandratinodum. Colony structure within nests is an important trait in ants, especially in the case of mixed societies, when host and parasite coexist in the same nest. Data for their respective free‐living hosts, Proformica korbi, P. longiseta and P. sp., are also provided. For our study, we integrated a meticulous excavation procedure with a genetic method. We conclude that the average number of parasites, as well as of slaves, is species‐specific, whereas nest depth depends on the nest architecture of the host. The genus Rossomyrmex seems to be monogynous and monandrous, whereas Proformica shows differences in the number of queens and mating frequency. R. quandratinodum shows different traits in nest composition (host/parasite ratio: P/R) and architecture. The difference in traits may account for some differences in parasitism: raid process or avoidance of parasitism.

Mechanistic target of rapamycin (mTOR) is a central component of the essential signaling pathway that regulates cell growth and proliferation by controlling anabolic processes in cells. mTOR exists in two distinct mTOR complexes known as mTORC1 and mTORC2 that reside mostly in cytoplasm. In our study, the biochemical characterization of mTOR led to discovery of its novel localization on nuclear envelope where it associates with a critical regulator of nuclear import Ran Binding Protein 2 (RanBP2). We show that association of mTOR with RanBP2 is dependent on the mTOR kinase activity that regulates the nuclear import of ribosomal proteins. The mTOR kinase inhibitors within thirty minutes caused a substantial decrease of ribosomal proteins in the nuclear but not cytoplasmic fraction. Detection of a nuclear accumulation of the GFP-tagged ribosomal protein rpL7a also indicated its dependence on the mTOR kinase activity. The nuclear abundance of ribosomal proteins was not affected by inhibition of mTOR Complex 1 (mTORC1) by rapamycin or deficiency of mTORC2, suggesting a distinctive role of the nuclear envelope mTOR complex in the nuclear import. Thus, we identified that mTOR in association with RanBP2 mediates the active nuclear import of ribosomal proteins.

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