A single PDZ domain protein interacts with the menkes copper ATPase, ATP7A : a new protein implicated in copper homeostasis Stephenson, Sarah E. M., Dubach, Daphne, Lim, Chris M., Mercer, Julian F. B. and La Fontaine, Sharon. 2005, A single PDZ domain protein interacts with the menkes copper ATPase, ATP7A : a new protein implicated in copper homeostasis, Journal of biological chemistry, vol. 280, no. 39, pp. 33270-33279, doi: 10.1074/jbc.M505889200. Attached Files Name Description MIMEType Size Downloads Title A single PDZ domain protein interacts with the menkes copper ATPase, ATP7A : a new protein implicated in copper homeostasis Author(s) Stephenson, Sarah E. M. Dubach, Daphne Lim, Chris M. orcid.org/0000-0002-5044-1539 Mercer, Julian F. B. La Fontaine, Sharon. orcid.org/0000-0002-9948-074X Journal name Journal of biological chemistry Volume number 280 Issue number 39 Start page 33270 End page 33279 Publisher American Society for Biochemistry and Molecular Biology Place of publication Baltimore, Md Publication date 2005-09-30 ISSN 0021-9258 1083-351X Summary The homeostatic regulation of essential elements such as copper requires many proteins whose activities are often mediated and tightly coordinated through protein-protein interactions. This regulation ensures that cells receive enough copper without intracellular concentrations reaching toxic levels. To date, only a small number of proteins implicated in copper homeostasis have been identified, and little is known of the protein-protein interactions required for this process. To identify other proteins important for copper homeostasis, while also elucidating the protein-protein interactions that are integral to the process, we have utilized a known copper protein, the copper ATPase ATP7A, as a bait in a yeast two-hybrid screen of a human cDNA library to search for interacting partners. One of the ATP7A-interacting proteins identified is a novel protein with a single PDZ domain. This protein was recently identified to interact with the plasma membrane calcium ATPase b-splice variants. We propose a change in name for this protein from PISP (plasma membrane calcium ATPase-interacting single-PDZ protein) to AIPP1 (ATPase-interacting PDZ protein) and suggest that it represents the protein that interacts with the class I PDZ binding motif identified at the ATP7A C terminus. The interaction in mammalian cells was confirmed and an additional splice variant of AIPP1 was identified. This study represents an essential step forward in identifying the proteins and elucidating the network of protein-protein interactions involved in maintaining copper homeostasis and validates the use of the yeast two-hybrid approach for this purpose. Language eng DOI 10.1074/jbc.M505889200 Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences HERDC Research category C1.1 Refereed article in a scholarly journal Copyright notice ©2005 by The American Society for Biochemistry and Molecular Biology, Inc. Free to Read? Yes Persistent URL http://hdl.handle.net/10536/DRO/DU:30039503 Document type: Journal Article Collections: Faculty of Science, Engineering and Built Environment School of Life and Environmental Sciences Open Access Collection Related Links Link Description Link to full-text (open access)   Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au. Versions Version Filter Type Wed, 26 Oct 2011, 10:40:04 EST Fri, 28 Oct 2011, 08:38:45 EST Fri, 28 Oct 2011, 08:41:21 EST Fri, 28 Oct 2011, 08:43:18 EST Fri, 13 Jun 2014, 11:28:39 EST Mon, 19 Jan 2015, 11:27:26 EST Fri, 06 Feb 2015, 10:47:35 EST Fri, 08 Nov 2019, 01:37:58 EST Tue, 23 Feb 2021, 11:35:17 EST Filtered Full Citation counts:   Cited 24 times in TR Web of Science Cited 25 times in Scopus Search Google Scholar Access Statistics: 609 Abstract Views, 0 File Downloads  -  Detailed Statistics Created: Wed, 26 Oct 2011, 10:40:04 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.