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E3 ubiquitin ligase RNF13 involves spatial learning and assembly of the SNARE complex

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 re... Full description

Journal Title: Cellular and Molecular Life Sciences 2013, Vol.70(1), pp.153-165
Main Author: Zhang, Qiang
Other Authors: Li, Yanfeng , Zhang, Lei , Yang, Nan , Meng, Jiao , Zuo, Pingping , Zhang, Yong , Chen, Jie , Wang, Li , Gao, Xiang , Zhu, Dahai
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 1420-682X ; E-ISSN: 1420-9071 ; DOI: 10.1007/s00018-012-1103-5
Link: http://dx.doi.org/10.1007/s00018-012-1103-5
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recordid: springer_jour10.1007/s00018-012-1103-5
title: E3 ubiquitin ligase RNF13 involves spatial learning and assembly of the SNARE complex
format: Article
creator:
  • Zhang, Qiang
  • Li, Yanfeng
  • Zhang, Lei
  • Yang, Nan
  • Meng, Jiao
  • Zuo, Pingping
  • Zhang, Yong
  • Chen, Jie
  • Wang, Li
  • Gao, Xiang
  • Zhu, Dahai
subjects:
  • RNF13
  • Ubiquitin ligase
  • Snapin
  • Synaptic vesicle
  • SNARE complex
ispartof: Cellular and Molecular Life Sciences, 2013, Vol.70(1), pp.153-165
description: 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.
language: eng
source:
identifier: ISSN: 1420-682X ; E-ISSN: 1420-9071 ; DOI: 10.1007/s00018-012-1103-5
fulltext: fulltext
issn:
  • 1420-9071
  • 14209071
  • 1420-682X
  • 1420682X
url: Link


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titleE3 ubiquitin ligase RNF13 involves spatial learning and assembly of the SNARE complex
creatorZhang, Qiang ; Li, Yanfeng ; Zhang, Lei ; Yang, Nan ; Meng, Jiao ; Zuo, Pingping ; Zhang, Yong ; Chen, Jie ; Wang, Li ; Gao, Xiang ; Zhu, Dahai
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descriptionChanges 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.
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abstractChanges 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.
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doi10.1007/s00018-012-1103-5
pages153-165
date2013-01