NDLI: The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).

Please wait, while we are loading the content...

Highly efficient uptake into cisplatin-resistant cells and the isomerization upon coordinative DNA binding of anticancer tetrazolato-bridged dinuclear platinum(II) complexes

Gene-specific regulation of hepatic selenoprotein expression by interleukin-6.

Synchrotron radiation based X-ray fluorescence shows changes in the elemental composition of the human substantia nigra in aged brains.

Year: 2015 Volume: 7 Issue: 10

Year: 2015 Volume: 7 Issue: 9

Year: 2015 Volume: 7 Issue: 8

Year: 2015 Volume: 7 Issue: 7

Year: 2015 Volume: 7 Issue: 6

Year: 2015 Volume: 7 Issue: 5

Year: 2015 Volume: 7 Issue: 4

Year: 2015 Volume: 7 Issue: 3

Year: 2015 Volume: 7 Issue: 2

Year: 2015 Volume: 7 Issue: 1

The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tsai, Cheng-Yu Liebig, Janika K. Tsigelny, Igor F. Howell, Stephen B.
Description	Country affiliation: United States Author Affiliation: Tsai CY ( Moores Cancer Center, University of California, San Diego, 3855 Health Sciences Drive, Mail Code 0819, La Jolla, CA 92093-0819, USA. showell@ucsd.edu.)
Abstract	Mammalian cells have two influx Cu transporters that form trimers in membranes. CTR1 is the high affinity transporter that resides largely in the plasma membrane, and CTR2 is the low affinity transporter that is primarily associated with vesicular structures inside the cell. The major differences between CTR1 and CTR2 are that CTR1 contains a HIS/MET-rich domain N-terminal of the METS that participate in the first two stacked rings that form the pore, and a longer C-terminal tail that includes a Cu binding HIS-CYS-HIS (HCH) motif right at the end. It has been reported that CTR1 and CTR2 are physically associated with each other in the cell. We used the CRISPR-Cas9 technology to knock out either CTR1 or CTR2 in fully malignant HEK293T and OVCAR8 human ovarian cancer cells to investigate the interaction of CTR1 and CTR2. We report here that the level of CTR2 protein is markedly decreased in CTR1 knockout clones while the CTR2 transcript level remains unchanged. CTR2 was found to be highly ubiquitinated in the CTR1 knock out cells, and inhibition of the proteasome prevented the degradation of CTR2 when CTR1 was not present while inhibition of autophagy had no effect. Re-expression of CTR1 rescued CTR2 from degradation in the CTR1 knockout cells. We conclude that CTR1 is essential to maintain the stability of CTR2 and that in the absence of CTR1 CTR2 is degraded by the proteasome. This reinforces the concept that the functions of CTR1 and CTR2 are inter-dependent within the Cu homeostasis system.
File Format	HTM / HTML
ISSN	17565901
e-ISSN	1756591X
DOI	10.1039/c5mt00131e
Journal	Metallomics
Issue Number	11
Volume Number	7
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2015-11-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Cation Transport Proteins Chemistry Metabolism Physiology Amino Acid Sequence Crispr-cas Systems Genetics Cell Line, Tumor Gene Knockout Techniques Hek293 Cells Molecular Sequence Data Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Copper Transporter 1 (CTR1) is Required to Maintain the Stability of Copper Transporter 2 (CTR2)

Copper transporters and chaperones CTR1, CTR2, ATOX1, and CCS as determinants of cisplatin sensitivity

Copper transporter 2 regulates intracellular copper and sensitivity to cisplatin

Gene duplication and neo-functionalization in the evolutionary and functional divergence of the metazoan copper transporters Ctr1 and Ctr2

Communication between the N and C termini is required for copper-stimulated Ser/Thr phosphorylation of Cu(I)-ATPase (ATP7B).

Ctr2 regulates biogenesis of a cleaved form of mammalian Ctr1 metal transporter lacking the copper- and cisplatin-binding ecto-domain.

Localization of copper and copper transporters in the human brain.

The Role of Ctr1 and Ctr2 in Mammalian Copper Homeostasis and Platinum-based Chemotherapy

Rate and Regulation of Copper Transport by Human Copper Transporter 1 (hCTR1)

The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).

Similar Documents

The Copper Transporter 1 (CTR1) is Required to Maintain the Stability of Copper Transporter 2 (CTR2)

Copper transporters and chaperones CTR1, CTR2, ATOX1, and CCS as determinants of cisplatin sensitivity

Copper transporter 2 regulates intracellular copper and sensitivity to cisplatin

Gene duplication and neo-functionalization in the evolutionary and functional divergence of the metazoan copper transporters Ctr1 and Ctr2

Communication between the N and C termini is required for copper-stimulated Ser/Thr phosphorylation of Cu(I)-ATPase (ATP7B).

Ctr2 regulates biogenesis of a cleaved form of mammalian Ctr1 metal transporter lacking the copper- and cisplatin-binding ecto-domain.

Localization of copper and copper transporters in the human brain.

The Role of Ctr1 and Ctr2 in Mammalian Copper Homeostasis and Platinum-based Chemotherapy

Rate and Regulation of Copper Transport by Human Copper Transporter 1 (hCTR1)

The copper transporter 1 (CTR1) is required to maintain the stability of copper transporter 2 (CTR2).