TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 284, NO. 1, pp. 696 –707, January 2, 2009 © 2009 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. COMMD1 Forms Oligomeric Complexes Targeted to the Endocytic Membranes via Specific Interactions with □ S Phosphatidylinositol 4,5-Bisphosphate Received for publication, June 23, 2008, and in revised form, October 7, 2008 Published, JBC Papers in Press, October 21, 2008, DOI 10.1074/jbc.M804766200 1 1 2 Jason L. Burkhead , Clinton T. Morgan , Ujwal Shinde, Gabrielle Haddock, and Svetlana Lutsenko From the Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239 Copper metabolism Murr1 domain 1 (COMMD1) is a 21-kDa of a gene mutated in dogs with severe hepatic copper toxicosis protein involved in copper export from the liver, NF-
B signal- (2). In several breeds of dogs, especially in Bedlington terriers, a ing, HIV infection, and sodium transport. The precise function mis-splicing event in the Murr1 gene results in the loss of pro- of COMMD and the mechanism through which COMMD1 per- tein expression (3) and massive copper accumulation in the forms its multiple roles are not understood. Recombinant liver that can reach remarkably high 
TI - COMMD1 Forms Oligomeric Complexes Targeted to the Endocytic Membranes via Specific Interactions with Phosphatidylinositol 4,5-Bisphosphate
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m804766200
DA - 2009-01-01
UR - https://www.deepdyve.com/lp/unpaywall/commd1-forms-oligomeric-complexes-targeted-to-the-endocytic-membranes-yNU0bywO6O
DP - DeepDyve
ER -