Cuprous binding promotes interaction of copper transport protein hCTR1 with cell membranes

Yang Yang; Yang Zhu; Hongze Hu; Lanjun Cheng; Manman Liu; Guolin Ma; Siming Yuan; Peixin Cui; Yangzhong Liu

doi:10.1039/c9cc04859f

Cuprous binding promotes interaction of copper transport protein hCTR1 with cell membranes

Chem Commun (Camb). 2019 Sep 21;55(74):11107-11110. doi: 10.1039/c9cc04859f. Epub 2019 Aug 28.

Authors

Yang Yang¹, Yang Zhu¹, Hongze Hu¹, Lanjun Cheng¹, Manman Liu¹, Guolin Ma², Siming Yuan¹, Peixin Cui³, Yangzhong Liu¹

Affiliations

¹ CAS High Magnetic Field Laboratory, Department of Chemistry, University of Science and Technology of China, Hefei Anhui, 230026, China. liuyz@ustc.edu.cn.
² Institute of Biosciences and Technology, College of Medicine, Texas A&M University, 2121 W Holcombe Blvd, Houston, TX 77030, USA.
³ Key Laboratory of Soil Environment and Pollution Remediation, Institute of Soil Science, the Chinese Academy of Sciences, Nanjing 210008, China.

PMID: 31461100
DOI: 10.1039/c9cc04859f

Abstract

Cu(i) binds to the N-terminal metal binding domain (MBD) of hCTR1 and induces its conformational change, which promotes the interaction of the MBD with cell membranes. The membrane interaction was confirmed in living cells. This process could be the first step to initiate the cellular uptake of copper ions by hCTR1.

MeSH terms

1,2-Dipalmitoylphosphatidylcholine / metabolism
Cell Line, Tumor
Cell Membrane / metabolism*
Copper / metabolism*
Copper Transporter 1 / metabolism*
Humans
Liposomes / metabolism*
Micelles
Molecular Dynamics Simulation
Peptide Fragments / metabolism*
Protein Binding
Protein Domains
Sodium Dodecyl Sulfate / metabolism

Substances

Copper Transporter 1
Liposomes
Micelles
Peptide Fragments
SLC31A1 protein, human
1,2-Dipalmitoylphosphatidylcholine
Sodium Dodecyl Sulfate
Copper