Copper Chaperone Atox1 Interacts with Cell Cycle Proteins
Journal article, 2018

The anaphase-promoting complex (APC) is involved in several processes in the cell cycle, most prominently it facilitates the separation of the sister chromatids during mitosis, before cell division. Because of the key role in the cell cycle, APC is suggested as a putative target for anticancer agents. We here show that the copper chaperone Atox1, known for shuttling copper in the cytoplasm from Ctr1 to ATP7A/B in the secretory pathway, interacts with several APC subunits. Atox1 interactions with APC subunits were discovered by mass spectrometry of co-immunoprecipitated samples and further confirmed using proximity ligation assays in HEK293T cells. Upon comparing wild-type cells with those in which the Atox1 gene had been knocked out, we found that in the absence of Atox1 protein, cells have prolonged G2/M phases and a slower proliferation rate. Thus, in addition to copper transport for loading of copper-dependent enzymes, Atox1 may modulate the cell cycle by interacting with APC subunits.

Cells

proteins

Cell proliferation

Mass spectrometry

Copper

Author

Maria Matson Dzebo

Chalmers, Biology and Biological Engineering, Chemical Biology

Stephanie Blockhuys

Chalmers, Biology and Biological Engineering, Chemical Biology

Sebastian Valenzuela

Chalmers, Biology and Biological Engineering, Chemical Biology

Emanuele Celauro

Chalmers, Biology and Biological Engineering, Chemical Biology

Elin Esbjörner Winters

Chalmers, Biology and Biological Engineering, Chemical Biology

Pernilla Wittung Stafshede

Chalmers, Biology and Biological Engineering, Chemical Biology

Computational and Structural Biotechnology Journal

2001-0370 (eISSN)

Vol. 16 443-449

Subject Categories

Cell Biology

Cell and Molecular Biology

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

DOI

10.1016/j.csbj.2018.10.018

More information

Latest update

11/20/2018