| First Author | Zhang Q | Year | 2013 |
| Journal | Cell Mol Life Sci | Volume | 70 |
| Issue | 1 | Pages | 153-65 |
| PubMed ID | 22890573 | Mgi Jnum | J:344668 |
| Mgi Id | MGI:6870659 | Doi | 10.1007/s00018-012-1103-5 |
| Citation | Zhang Q, et al. (2013) E3 ubiquitin ligase RNF13 involves spatial learning and assembly of the SNARE complex. Cell Mol Life Sci 70(1):153-65 |
| abstractText | Changes in the structure and number of synapses modulate learning, memory and cognitive disorders. Ubiquitin-mediated protein modification is a key mechanism for regulating synaptic activity, though the precise control of this process remains poorly understood. RING finger protein 13 (RNF13) is a recently identified E3 ubiquitin ligase, and its in vivo function remains completely unknown. We show here that genetic deletion of RNF13 in mice leads to a significant deficit in spatial learning as determined by the Morris water maze test and Y-maze learning test. At the ultrastructral level, the synaptic vesicle density was decreased and the area of the active zone was increased at hippocampal synapses of RNF13-null mice compared with those of wild-type littermates. We found no change in the levels of SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor) complex proteins in the hippocampus of RNF13-null mice, but impaired SNARE complex assembly. RNF13 directly interacted with snapin, a SNAP-25-interacting protein. Interestingly, snapin was ubiquitinated by RNF13 via the lysine-29 conjugated polyubiquitin chain, which in turn promoted the association of snapin with SNAP-25. Consistently, we found an attenuated interaction between snapin and SNAP-25 in the RNF13-null mice. Therefore, these results suggest that RNF13 is involved in the regulation of the SNARE complex, which thereby controls synaptic function. |
