Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family
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Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family Taniya Mandal1 · Sumanta Kar1 · Saptarshi Maji1 · Samarpita Sen1 · Arnab Gupta1 Received: 20 July 2020 / Accepted: 4 September 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Copper is crucial for carrying out normal physiological functions in all higher life forms. Copper Transporter 1 (CTR1) is the high-affinity copper importer found in all eukaryotic organisms. The copper transporter family primarily comprises ~ six members (CTR1-6) and the related members share high sequence homology with CTR. However, with the exception of CTR1, not all six CTRs are present in every organism. Despite having a simple trimeric channel structure, CTR1 and other members exhibit some unique regulatory properties. In the present review, we attempt to understand the diversity and similarity of regulation and functioning of the members of this copper transporter family. Graphic Abstract
Keywords Copper · Copper Transporter · CTR
Introduction Copper is essential for growth and development; however, in excess it is harmful. All eukaryotic organisms require copper for various metabolic activities. Copper serves as an Taniya Mandal, Sumanta Kar, Saptarshi Maji and Samarpita Sen have Contributed equally to this manuscript * Arnab Gupta [email protected] 1
Department of Biological Sciences, Indian Institute of Science Education and Research Kolkata, Mohanpur 741246, India
essential cofactor for the activity of cytochrome C oxidase in mitochondria, an enzyme essential for respiration, and for Cu, Zn-superoxide dismutase that detoxifies oxygen radicals in the cytosol. In addition, copper is also intrinsically linked to the secretory pathway, where enzymes including dopamine-β-hydroxylase, peptidyl α-monooxygenase, ceruloplasmin, and tyrosinase incorporate copper as a cofactor in their catalytic sites (Lutsenko et al 2007). Key proteins maintaining optimum copper levels in mammalian cells include the homotrimeric plasma membrane copper importer, Copper Transporter 1 (CTR1), and ATP-driven copper export pumps, ATP7 in lower organisms that diverges as ATP7A and ATP7B in chordates (Gupta and Lutsenko 2012). CTR1
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is the only high-affinity copper transporter that is primarily localized in the plasma membrane and draws copper from the extracellular space (Clifford et al 2016). CTR1 is a unique and interesting protein, not only because of its biological importance but also in the unconventional fashion that it is regulated. CTR1 belongs to a family of Copper Transporters that has at least six members (CTR1-6) among various organisms. Structural and functional divergence of the CTRs from lower organisms to mammals shed light on how the regulation of this protein family is modulated depending on the requirement and availability of copper. This review article from a phylogenetic viewpoint summarizes and critically analyses the advancements to understand the regulation of C
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