Enhancement of visual biological motion recognition in early-deaf adults: Functional and behavioral correlates.

Deafness leads to brain modifications that are generally associated with a cross-modal activity of the auditory cortex, particularly for visual stimulations. In the present study, we explore the cortical processing of biological motion that conveyed either non-communicative (pantomimes) or communicative (emblems) information, in early-deaf and hearing individuals, using fMRI analyses. Behaviorally, deaf individuals showed an advantage in detecting communicative gestures relative to hearing individuals. Deaf individuals also showed significantly greater activation in the superior temporal cortex (including the planum temporale and primary auditory cortex) than hearing individuals. The activation levels in this region were correlated with deaf individuals' response times. This study provides neural and behavioral evidence that cross-modal plasticity leads to functional advantages in the processing of biological motion following lifelong auditory deprivation.

Arabidopsis CIPK26 interacts with KEG, components of the ABA signalling network and is degraded by the ubiquitin-proteasome system.

The RING-type E3 ligase, Keep on Going (KEG), is required for early seedling establishment in Arabidopsis thaliana. Post-germination, KEG negatively regulates abscisic acid (ABA) signalling by targeting Abscisic Acid Insensitive 5 (ABI5) for ubiquitination and subsequent degradation. Previous reports suggest that the role of KEG during early seedling development is not limited to regulation of ABI5 abundance. Using a yeast two-hybrid screen, this study identified Calcineurin B-like Interacting Protein Kinase (CIPK) 26 as a KEG-interacting protein. In vitro pull-down and in planta bimolecular fluorescence complementation assays confirmed the interactions between CIPK26 and KEG. In planta experiments demonstrated that CIPK26 was ubiquitinated and degraded via the 26S proteasome. It was also found that turnover of CIPK26 was increased when KEG protein levels were elevated, suggesting that the RING-type E3 ligase is involved in targeting CIPK26 for degradation. CIPK26 was found to interact with the ABA signalling components ABI1, ABI2, and ABI5. In addition, CIPK26 was capable of phosphorylating ABI5 in vitro. Consistent with a role in ABA signalling, overexpression of CIPK26 increased the sensitivity of germinating seeds to the inhibitory effects of ABA. The data presented in this report suggest that KEG mediates the proteasomal degradation of CIPK26 and that CIPK26 is part of the ABA signalling network.