SUMOylation of synaptic and synapse‐associated proteins: An update. Issue 2 (5th July 2020)
- Record Type:
- Journal Article
- Title:
- SUMOylation of synaptic and synapse‐associated proteins: An update. Issue 2 (5th July 2020)
- Main Title:
- SUMOylation of synaptic and synapse‐associated proteins: An update
- Authors:
- Henley, Jeremy M.
Seager, Richard
Nakamura, Yasuko
Talandyte, Karolina
Nair, Jithin
Wilkinson, Kevin A. - Abstract:
- Abstract: SUMOylation is a post‐translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein–protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear proteins, SUMOylation of extranuclear proteins contributes to the control of neuronal development, neuronal stress responses and synaptic transmission and plasticity. In this brief review we provide an update of recent developments in the identification of synaptic and synapse‐associated SUMO target proteins and discuss the cell biological and functional implications of these discoveries. Abstract : In this Review, we highlight advances in the field of neuronal SUMOylation and discuss how SUMOylation regulates processes within pre‐ and post‐synapses. Enhanced SUMOylation of Na + channels increases conductance and SUMO‐modified collapsin response mediator protein 2 stabilizes Na + channel surface expression. DeSUMOylation of metabotropic glutamate receptors mGluR7 promotes internalization. At the post‐synapse, GluK2 activation leads to SUMOylation and internalization. mGluR activation leads to accumulation of Ubc9, but can also enhance SENP1 levels, likely leading to homeostatic SUMO modulation. Downstream effects include regulation of actin dynamics, increasing AMPA receptor expression and local translation. These findings provide new appreciation of the roles ofAbstract: SUMOylation is a post‐translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein–protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear proteins, SUMOylation of extranuclear proteins contributes to the control of neuronal development, neuronal stress responses and synaptic transmission and plasticity. In this brief review we provide an update of recent developments in the identification of synaptic and synapse‐associated SUMO target proteins and discuss the cell biological and functional implications of these discoveries. Abstract : In this Review, we highlight advances in the field of neuronal SUMOylation and discuss how SUMOylation regulates processes within pre‐ and post‐synapses. Enhanced SUMOylation of Na + channels increases conductance and SUMO‐modified collapsin response mediator protein 2 stabilizes Na + channel surface expression. DeSUMOylation of metabotropic glutamate receptors mGluR7 promotes internalization. At the post‐synapse, GluK2 activation leads to SUMOylation and internalization. mGluR activation leads to accumulation of Ubc9, but can also enhance SENP1 levels, likely leading to homeostatic SUMO modulation. Downstream effects include regulation of actin dynamics, increasing AMPA receptor expression and local translation. These findings provide new appreciation of the roles of SUMOylation in synaptic function and plasticity. … (more)
- Is Part Of:
- Journal of neurochemistry. Volume 156:Issue 2(2021)
- Journal:
- Journal of neurochemistry
- Issue:
- Volume 156:Issue 2(2021)
- Issue Display:
- Volume 156, Issue 2 (2021)
- Year:
- 2021
- Volume:
- 156
- Issue:
- 2
- Issue Sort Value:
- 2021-0156-0002-0000
- Page Start:
- 145
- Page End:
- 161
- Publication Date:
- 2020-07-05
- Subjects:
- GTPases -- ion channels -- SUMOylation -- synaptic plasticity -- synaptic proteins
Neurochemistry -- Periodicals
616.8042 - Journal URLs:
- http://www.blackwell-synergy.com/loi/jnc ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/jnc.15103 ↗
- Languages:
- English
- ISSNs:
- 0022-3042
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5021.500000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 15564.xml