Training Improves Vibrotactile Spatial Acuity and Intensity Discrimination on the Lower Back Using Coin Motors

Tactile vision substitution devices are assistive technologies for the blind that redirect visual information to the tactile sense. They typically include a tactile display that conveys visual information to the skin. Two important parameters that determine the maximum information bandwidth of tactile displays are the spatial acuity of the skin, and the ability of the user to discriminate between stimulus intensities. These two parameters were investigated by determining the two‐point discrimination (TPD) threshold and the just‐noticeable intensity difference (JND) using coin motors on the lower back. Coin motors are eccentric rotating‐mass motors that are affordable, energy‐efficient, and easy to implement. The lower back was chosen because it is a discreet place to wear assistive technology. It is generally available for use, as it is usually not critically involved in activities of daily living. Rehabilitation with sensory substitution devices often requires training by professional occupational therapists, because the user needs to extract visual information from sparse information presented through an alternative channel such as the skin. In this study they determined whether short, automated training sessions of 5 min each could improve the TPD threshold and JND. It was found that 10 min of computer‐assisted training improved the vibrotactile TPD threshold on the lower back by 36%, and that 18 min of training improved the just‐noticeable intensity difference (JND) by 44%. It was concluded that short, automated training sessions could provide a fast and inexpensive means to improve people's basic spatial acuity and intensity discrimination skills with coin motors.NICTA is funded by the Australian Government through the Department of Communications and the Australian Research Council through the ICT Centre of Excellence Program. NICTA is also funded and supported by the Australian Capital Territory, the New South Wales, Queensland and Victorian Governments, the Australian National University, the University of New South Wales, the University of Melbourne, the University of Queensland, the University of Sydney Griffith University, Queensland University of Technology, Monash University, and other university partner

LIP5 Interacts with Aquaporin 2 and Facilitates Its Lysosomal Degradation

Vasopressin binding to the V2 receptor in renal principal cells leads to activation of protein kinase A, phosphorylation of aquaporin 2 (AQP2) at Ser256, and the translocation of AQP2 to the apical membrane, resulting in concentration of the urine. In contrast, phorbol ester–induced activation of protein kinase C pathway leads to ubiquitination of AQP2 at Lys270 and its internalization to multivesicular bodies, where it is targeted for lysosomal degradation or stored for recycling. Because little is known about the regulation of AQP2 trafficking, we used the carboxy-terminal tail of constitutively nonphosphorylated AQP2 (S256A) as a bait for interacting proteins in a yeast two-hybrid assay. We isolated lysosomal trafficking regulator–interacting protein 5 (LIP5) and found that LIP5 interacted with the proximal carboxy-terminal tail (L230-D243) of AQP2 in vitro but not with AQP3 or AQP4, which are also expressed in principal cells. Immunohistochemistry revealed that LIP5 co-localized with AQP2 in principal cells. LIP5 binding occurred independent of the state of Ser256 phosphorylation or Lys270 ubiquitination. LIP5 has been shown to facilitate degradation of the EGF receptor; here, LIP5 seemed to bind this receptor. Knockdown of LIP5 in mouse renal cells (mpkCCD) reduced the phorbol ester–induced degradation of AQP2 approximately two-fold. In summary, LIP5 binds cargo proteins and, considering the role of LIP5 in protein sorting to multivesicular bodies, plays a role in the degradation of AQP2, possibly by reducing the formation of late endosomes