scholarly journals Human copper transporter ATP7B (Wilson disease protein) forms stable dimersin vitroand in cells

2017 ◽  
Vol 292 (46) ◽  
pp. 18760-18774 ◽  
Author(s):  
Samuel Jayakanthan ◽  
Lelita T. Braiterman ◽  
Nesrin M. Hasan ◽  
Vinzenz M. Unger ◽  
Svetlana Lutsenko
Keyword(s):  
Wilson Disease ◽  
Copper Transporter ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
In Cells

scholarly journals Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments

1997 ◽  
Vol 326 (3) ◽  
pp. 897-902 ◽  
Author(s):  
Xiao-Li YANG ◽  
Naoyuki MIURA ◽  
Yoshihiko KAWARADA ◽  
Kunihiko TERADA ◽  
Konstantin PETRUKHIN ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Wilson Disease ◽  
Intracellular Transport ◽  
Copper Metabolism ◽  
Copper Transporter ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
Human Disorders ◽  
P Type ◽  
Cellular Compartments

Copper is an essential trace element in prokaryotes and eukaryotes and is strictly regulated by biological mechanisms. Menkes and Wilson diseases are human disorders that arise from disruption of the normal process of copper export from the cytosol to the extracellular environment. Recently a gene for Wilson disease (WD) (also named the ATP7B gene) was cloned. This gene encodes a copper transporter of the P-type ATPase. We prepared monoclonal and polyclonal anti-(WD protein) antibodies and characterized the full-length WD protein as well as a shorter form that is produced by alternative splicing in the human brain. We found that the WD protein is localized mainly in the Golgi apparatus, whereas the shorter form is present in the cytosol. These results suggest that the alternative WD proteins act as key regulators of copper metabolism, perhaps by performing distinct roles in the intracellular transport and export of copper.

scholarly journals Retromer retrieves the Wilson disease protein ATP7B from endolysosomes in a copper-dependent manner

2020 ◽  
Vol 133 (24) ◽  
pp. jcs246819 ◽  
Author(s):  
Santanu Das ◽  
Saptarshi Maji ◽  
Ruturaj ◽  
Indira Bhattacharya ◽  
Tanusree Saha ◽  
...  
Keyword(s):  
Wilson Disease ◽  
Dependent Manner ◽  
Copper Transporter ◽  
Copper Chelation ◽  
Trans Golgi Network ◽  
Wilson Disease Protein ◽  
Retromer Complex ◽  
High Copper ◽  
Disease Protein ◽  
Golgi Network

ABSTRACTThe Wilson disease protein, ATP7B maintains copper (herein referring to the Cu+ ion) homeostasis in the liver. ATP7B traffics from trans-Golgi network to endolysosomes to export excess copper. Regulation of ATP7B trafficking to and from endolysosomes is not well understood. We investigated the fate of ATP7B after copper export. At high copper levels, ATP7B traffics primarily to acidic, active hydrolase (cathepsin-B)-positive endolysosomes and, upon subsequent copper chelation, returns to the trans-Golgi network (TGN). At high copper, ATP7B colocalizes with endolysosomal markers and with a core member of retromer complex, VPS35. Knocking down VPS35 did not abrogate the copper export function of ATP7B or its copper-responsive anterograde trafficking to vesicles; rather upon subsequent copper chelation, ATP7B failed to relocalize to the TGN, which was rescued by overexpressing wild-type VPS35. Overexpressing mutants of the retromer complex-associated proteins Rab7A and COMMD1 yielded a similar non-recycling phenotype of ATP7B. At high copper, VPS35 and ATP7B are juxtaposed on the same endolysosome and form a large complex that is stabilized by in vivo photoamino acid labeling and UV-crosslinking. We demonstrate that retromer regulates endolysosome to TGN trafficking of copper transporter ATP7B in a manner that is dependent upon intracellular copper.

Small pH and Salt Variations Radically Alter the Thermal Stability of Metal-Binding Domains in the Copper Transporter, Wilson Disease Protein

2013 ◽  
Vol 117 (42) ◽  
pp. 13038-13050 ◽  
Author(s):  
Lina Nilsson ◽  
Jörgen Ådén ◽  
Moritz S. Niemiec ◽  
Kwangho Nam ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Thermal Stability ◽  
Metal Binding ◽  
Wilson Disease ◽  
Copper Transporter ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
Disease Protein ◽  
Thermal Stability Of

Localization of the Wilson disease protein in murine intestine

2008 ◽  
Vol 46 (09) ◽  
Author(s):  
KH Weiss ◽  
D Gotthardt ◽  
J Wurz ◽  
U Merle ◽  
W Stremmel ◽  
...  
Keyword(s):  
Wilson Disease ◽  
Wilson Disease Protein ◽  
Disease Protein

Translocation of the Wilson disease protein ATP7B is independent of Murr1/ COMMD1 and Rab7

2008 ◽  
Vol 46 (01) ◽  
Author(s):  
KH Weiss ◽  
JC Lozoya ◽  
S Tuma ◽  
D Gotthardt ◽  
J Reichert ◽  
...  
Keyword(s):  
Wilson Disease ◽  
Wilson Disease Protein ◽  
Disease Protein

scholarly journals Cu(I) Binding and Transfer by the N Terminus of the Wilson Disease Protein

2007 ◽  
Vol 282 (12) ◽  
pp. 8622-8631 ◽  
Author(s):  
Liliya A. Yatsunyk ◽  
Amy C. Rosenzweig
Keyword(s):  
Wilson Disease ◽  
Wilson Disease Protein ◽  
N Terminus ◽  
Disease Protein

scholarly journals Analysis of functional domains of Wilson disease protein (ATP7B) in Saccharomyces cerevisiae

FEBS Letters ◽  
1998 ◽  
Vol 428 (3) ◽  
pp. 281-285 ◽  
Author(s):  
Masatake Iida ◽  
Kunihiko Terada ◽  
Yoshihiro Sambongi ◽  
Tokumitsu Wakabayashi ◽  
Naoyuki Miura ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Wilson Disease ◽  
Functional Domains ◽  
Wilson Disease Protein ◽  
Disease Protein

scholarly journals Copper relay path through the N-terminus of Wilson disease protein, ATP7B

Metallomics ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 1472-1480 ◽  
Author(s):  
Kumaravel Ponnandai Shanmugavel ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Metal Binding ◽  
Wilson Disease ◽  
Copper Transport ◽  
Binding Domains ◽  
Wilson Disease Protein ◽  
N Terminus ◽  
Disease Protein ◽  
Yeast Assay

Using a yeast assay, we identified the roles of ATP7B's six metal-binding domains in internal copper transport and soluble chaperone capacity.

scholarly journals Copper-Induced Translocation of the Wilson Disease Protein ATP7B Independent of Murr1/COMMD1 and Rab7

2008 ◽  
Vol 173 (6) ◽  
pp. 1783-1794 ◽  
Author(s):  
Karl Heinz Weiss ◽  
Javier Carbajo Lozoya ◽  
Sabine Tuma ◽  
Daniel Gotthardt ◽  
Jürgen Reichert ◽  
...  
Keyword(s):  
Wilson Disease ◽  
Wilson Disease Protein ◽  
Disease Protein
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