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Type: Journal article
Title: N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel golgi-associated protein
Author: Harvey, K.
Shearwin-Whyatt, L.
Fotia, A.
Parton, R.
Kumar, S.
Citation: Journal of Biological Chemistry, 2002; 277(11):9307-9317
Publisher: Amer Soc Biochemistry Molecular Biology Inc
Issue Date: 2002
ISSN: 0021-9258
Statement of
Kieran F. Harvey, Linda M. Shearwin-Whyatt, Andrew Fotia, Robert G. Parton and Sharad Kumar
Abstract: Nedd4 belongs to a family of ubiquitin-protein ligases that is characterized by 2--4 WW domains, a carboxyl-terminal Hect (homologous to E6-AP Carboxyl terminus)domain and in most cases an amino-terminal C2 domain. We had previously identified a series of proteins that associates with the WW domains of Nedd4. In this paper, we demonstrate that one of the Nedd4-binding proteins, N4WBP5, belongs to a small group of evolutionarily conserved proteins with three transmembrane domains. N4WBP5 binds Nedd4 WW domains via the two PPXY motifs present in the amino terminus of the protein. In addition to Nedd4, N4WBP5 can interact with the WW domains of a number of Nedd4 family members and is ubiquitinated. Endogenous N4WBP5 localizes to the Golgi complex. Ectopic expression of the protein disrupts the structure of the Golgi, suggesting that N4WBP5 forms part of a family of integral Golgi membrane proteins. Based on previous observations in yeast, we propose that N4WBP5 may act as an adaptor for Nedd4-like proteins and their putative targets to control ubiquitin-dependent protein sorting and trafficking.
Keywords: Golgi Apparatus
Ubiquitin-Protein Ligases
Intercellular Signaling Peptides and Proteins
Carrier Proteins
Calcium-Binding Proteins
Membrane Proteins
RNA, Messenger
Amino Acid Sequence
Molecular Sequence Data
Endosomal Sorting Complexes Required for Transport
Nedd4 Ubiquitin Protein Ligases
DOI: 10.1074/jbc.M110443200
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