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.
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Acknowledgements
This work was supported by Wellcome Trust India Alliance Fellowship (IA/I/16/1/502369) and Early Career Research Award (ECR/2015/000220) from SERB, Department of Science and Technology (DST), Government of India and IISER K intramural funding to AG. SM and SK were supported by Predoctoral fellowships from Council of Scientific and Industrial Research, India. TM and SS were supported by KVPY fellowship from the Govt. of India.
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Mandal, T., Kar, S., Maji, S. et al. Structural and Functional Diversity Among the Members of CTR, the Membrane Copper Transporter Family. J Membrane Biol 253, 459–468 (2020). https://doi.org/10.1007/s00232-020-00139-w
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DOI: https://doi.org/10.1007/s00232-020-00139-w