Document Detail


Regulation of the hDlg/hScrib/Hugl-1 tumour suppressor complex.
MedLine Citation:
PMID:  18793635     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The proper function of the Scribble tumour suppressor complex is dependent upon the correct localisation of its components. Previously we observed dynamic relocalisation of the hDlg component under conditions of osmotic stress. We now show that the other two components of the complex, hScrib and Hugl-1 display similar patterns of expression. We demonstrate, by shRNA ablation of hScrib expression, that hDlg and Hugl-1 are in part dependent upon hScrib for their correct localization. However under conditions of osmotic stress this apparent dependency no longer exists: hDlg and Hugl-1 localise to cell membranes independently of hScrib. We also demonstrate an interaction between the three components of the hScrib complex and the tSNARE syntaxin 4, and show that correct localization of the Scrib complex is in part tSNARE dependent. This is the first detailed analysis of the co-localisation and function of the hScrib complex in mammalian cells and demonstrates a direct link between the control of the hScrib complex and vesicle transport pathways.
Authors:
Paola Massimi; Nisha Narayan; Miranda Thomas; Noor Gammoh; Susanne Strand; Dennis Strand; Lawrence Banks
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-09-03
Journal Detail:
Title:  Experimental cell research     Volume:  314     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-10-30     Completed Date:  2008-12-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3306-17     Citation Subset:  IM    
Affiliation:
International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy. paola@icgeb.org
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MeSH Terms
Descriptor/Qualifier:
Adaptor Proteins, Signal Transducing / antagonists & inhibitors,  genetics,  metabolism*
Animals
Blotting, Western
Cell Line
Cytoskeletal Proteins / metabolism*
Gene Expression Regulation / drug effects,  physiology*
Humans
Membrane Proteins / antagonists & inhibitors,  genetics,  metabolism*
Multiprotein Complexes / metabolism
Osmolar Concentration
Protein Transport / drug effects,  physiology
Qa-SNARE Proteins / metabolism
RNA Interference
Signal Transduction / drug effects
Sorbitol / pharmacology
Transport Vesicles / physiology
Tumor Suppressor Proteins / antagonists & inhibitors,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Cytoskeletal Proteins; 0/DLG1 protein, human; 0/LLGL1 protein, human; 0/Membrane Proteins; 0/Multiprotein Complexes; 0/Qa-SNARE Proteins; 0/SCRIB protein, human; 0/Tumor Suppressor Proteins; 50-70-4/Sorbitol

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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