Watt, NT, Griffiths, HH orcid.org/0000-0001-5154-4815 and Hooper, NM (2013) Neuronal zinc regulation and the prion protein. Prion, 7 (3). pp. 203-208. ISSN 1933-6896
Abstract
Zinc, the most abundant trace metal in the brain, has numerous functions in health and disease. It is released into the synaptic cleft alongside glutamate and this connection between zinc and glutamatergic neurotransmission allows the ion to modulate overall excitability of the brain and influence synaptic plasticity. To maintain healthy synapses, extracellular zinc levels need to be tightly regulated. We recently reported that the cellular prion protein (PrPC) can directly influence neuronal zinc concentrations by promoting zinc uptake via AMPA receptors. The octapeptide repeat region of PrPC is involved in zinc sensing or scavenging and the AMPA receptor provides the channel for transport of the metal across the membrane, facilitated by a direct interaction between the N-terminal polybasic region of PrPC and AMPA receptors. PrPC has been evolutionarily linked to the Zrt/Irt-like protein (ZIP) metal ion transport family with the C-terminus of PrPC sharing sequence similarities with the N-terminal extracellular domains of ZIP 5, 6 and 10. By incorporating the properties of ZIP transporters (both zinc sensing and zinc transport) into two existing neuronal proteins, (PrPC as zinc sensor, AMPA receptor as zinc transporter), neuronal cells are enhancing their biological efficiency and functionality.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2013 Landes Bioscience. This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. To view a copy of this license, visit https://creativecommons.org/licenses/by-nc/3.0/. |
Keywords: | prion; zinc; AMPA receptor; ZIP transporter |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 06 Aug 2018 14:09 |
Last Modified: | 06 Aug 2018 14:09 |
Status: | Published |
Publisher: | Taylor & Francis |
Identification Number: | 10.4161/pri.24503 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:134112 |
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