skip to main content
Guest
My Research
My Account
Sign out
Sign in
This feature requires javascript
Library Search
Find Databases
Browse Search
E-Journals A-Z
E-Books A-Z
Citation Linker
Help
Language:
English
Vietnamese
This feature required javascript
This feature requires javascript
Primo Search
All Library Resources
All
Course Materials
Course Materials
Search For:
Clear Search Box
Search in:
All Library Resources
Or hit Enter to replace search target
Or select another collection:
Search in:
All Library Resources
Search in:
Print Resources
Search in:
Digital Resources
Search in:
Online E-Resources
Advanced Search
Browse Search
This feature requires javascript
Search Limited to:
Search Limited to:
Resource type
criteria input
All items
Books
Articles
Images
Audio Visual
Maps
Graduate theses
Show Results with:
criteria input
that contain my query words
with my exact phrase
starts with
Show Results with:
Search type Index
criteria input
anywhere in the record
in the title
as author/creator
in subject
Full Text
ISBN
ISSN
TOC
Keyword
Field
Show Results with:
in the title
Show Results with:
anywhere in the record
in the title
as author/creator
in subject
Full Text
ISBN
ISSN
TOC
Keyword
Field
This feature requires javascript
Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells
The FASEB journal, 2009-06, Vol.23 (6), p.1935-1945
[Peer Reviewed Journal]
FASEB ;2009 FASEB 2009 ;ISSN: 0892-6638 ;EISSN: 1530-6860 ;DOI: 10.1096/fj.08-121947 ;PMID: 19193720
Full text available
Citations
Cited by
View Online
Details
Recommendations
Reviews
Times Cited
External Links
This feature requires javascript
Actions
Add to My Research
Remove from My Research
E-mail
Print
Permalink
Citation
EasyBib
EndNote
RefWorks
Delicious
Export RIS
Export BibTeX
This feature requires javascript
Title:
Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells
Author:
Zeng, Fenghua
;
Xu, Jie
;
Harris, Raymond C
Subjects:
Amino Acid Motifs
;
Animals
;
Cells, Cultured
;
Dogs
;
E3 ubiquitin ligase
;
Endosomal Sorting Complexes Required for Transport
;
Enzyme Inhibitors - metabolism
;
Humans
;
Lysosomes - metabolism
;
Mutagenesis, Site-Directed
;
Nedd4 Ubiquitin Protein Ligases
;
nuclear translocation
;
PI3 kinase
;
Proteasome Endopeptidase Complex - metabolism
;
Proteasome Inhibitors
;
Protein Isoforms - genetics
;
Protein Isoforms - metabolism
;
Protein Structure, Tertiary
;
PY motif mutation
;
Receptor, Epidermal Growth Factor - genetics
;
Receptor, Epidermal Growth Factor - metabolism
;
Receptor, ErbB-4
;
Recombinant Fusion Proteins - genetics
;
Recombinant Fusion Proteins - metabolism
;
Research Communications
;
Tetradecanoylphorbol Acetate - metabolism
;
Ubiquitin - metabolism
;
Ubiquitin-Protein Ligases - genetics
;
Ubiquitin-Protein Ligases - metabolism
;
Ubiquitination
Is Part Of:
The FASEB journal, 2009-06, Vol.23 (6), p.1935-1945
Description:
ErbB4, a type I transmembrane receptor tyrosine kinase, is a member of the epidermal growth factor receptor family. Its cleavage releases an intracellular C-terminal domain (ICD), which can be either degraded following ubiqitination or translocated to the nucleus and regulate gene expression. There are 2 ErbB4 ICD isoforms: CYT-1 and CYT-2. We and others have previously reported that following cleavage, CYT-2 selectively translocates to the nucleus. In the current study we found that following cleavage, the intracellular levels of CYT-1 ICD decreased rapidly, while levels of CYT-2 ICD remained relatively stable. CYT-1 ICD degradation could be prevented by administration of either the proteasome inhibitor lactacystin or the lysosome inhibitor chloroquine, indicating both proteasomal and lysosomal degradation. Further studies implicated Nedd4, an E3 ubiquitin ligase, as a mediator of CYT-1 ubiquitination and degradation. The interaction of Nedd4 with CYT-1 was shown by coimmnunoprecipitation, an in vitro direct binding assay, and an in vitro ubiquitination assay. Three PPxY or PY motifs present in the CYT-1 C terminus are necessary for binding by Nedd4 WW domains, because impaired interactions are seen in mutation of any of the PY motifs. Nedd4-CYT-1 binding was associated with increased CYT-1 ubiquitination following proteasome inhibitor treatment. Impaired Nedd4 binding to CYT-1 by PY motif mutations led to increased CYT-1 ICD stability, whereas only one of the PY motif mutations (Y1056A), which disrupts the binding sites for both a WW domain and an SH2 domain of PI3 kinase, demonstrated enhanced nuclear translocation following HB-EGF treatment. These studies indicate that Nedd4 mediates ErbB4 CYT-1 ICD ubiquitination and degradation, and the prevention of both WW binding and PI3 kinase activity are required for ErbB4 nuclear translocation.--Zeng, F., Xu, J., Harris, R. C. Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells.
Publisher:
United States: The Federation of American Societies for Experimental Biology
Language:
English
Identifier:
ISSN: 0892-6638
EISSN: 1530-6860
DOI: 10.1096/fj.08-121947
PMID: 19193720
Source:
MEDLINE
Alma/SFX Local Collection
This feature requires javascript
This feature requires javascript
Back to results list
This feature requires javascript
This feature requires javascript
Searching Remote Databases, Please Wait
Searching for
in
scope:(TDTS),scope:(SFX),scope:(TDT),scope:(SEN),primo_central_multiple_fe
Show me what you have so far
This feature requires javascript
This feature requires javascript