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Nuclear export of proteins and ribonucleoproteins is mediated by the CRM1/RANBP2-5/ESCRT-I nuclear export complex. The export pathway consists of a nucleoporin ring (Nup62-160/Nup205), an adaptor protein (Nup62), and the export receptor subunit Ran-binding protein 2 (RanBP2). We have shown that RanBP2 also binds small molecule compounds. We have characterized, in vitro, the interactions of the RanBP2 C-terminal region (RanBP2-5) and the small molecule compound dihydrotestosterone, which in vivo binds the same site, with full-length RanBP2, Nup205, and the RanBP2-5 truncation variants. Our results indicate that the dihydrotestosterone molecule binds to the same site as Nup205, and that the compound’s binding is mediated by Nup62 and RanBP2. Full-length RanBP2-5 forms a stable complex with Nup62 and RanBP2 when RanBP2-5 is in excess, which dissociates when RanBP2-5 is in limiting concentrations. We further demonstrate that the RanBP2 C-terminal region binds dihydrotestosterone in a manner that is competitive with Nup62 and dependent upon concentration of both Nup62 and RanBP2-5. Here we describe for the first time the structure of the RanBP2-5/ESCRT-I/Nup62/Nup145C export complex and describe its interactions with the RanBP2 C-terminal region, thereby providing the basis for functional studies.Perceptual and psychophysical properties of a tool for the quantification of the association between the hand and the keyboard.
This study aims to develop a tool for the quantification of the hand-keyboard association. The tool developed was compared to the tasks of the Physical Activity Limitation Scale for Individuals with Handicaps. Hand and keyboard tests were performed while participants were seated in front of a computer (a distance of 25 cm). The range of motion of both upper limbs was recorded during the administration of
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