Document Detail


Alix regulates cortical actin and the spatial distribution of endosomes.
MedLine Citation:
PMID:  15914539     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Alix/AIP1 is a proline-rich protein that has been implicated in apoptosis, endocytic membrane trafficking and viral budding. To further elucidate the functions of Alix, we used RNA interference to specifically suppress its expression. Depletion of Alix caused a striking redistribution of early endosomes from a peripheral to a perinuclear location. The redistribution of endosomes did not affect transferrin recycling or degradation of endocytosed epidermal growth factor receptors, although the uptake of transferrin was mildly reduced when Alix was downregulated. Quantitative immunoelectron microscopy showed that multivesicular endosomes of Alix-depleted cells contained normal amounts of CD63, whereas their levels of lysobisphosphatidic acid were reduced. Alix depletion also caused an accumulation of unusual actin structures that contained clathrin and cortactin, a protein that couples membrane dynamics to the cortical actin cytoskeleton. Our results suggest that Alix functions in the actin-dependent intracellular positioning of endosomes, but that it is not essential for endocytic recycling or for trafficking of membrane proteins between early and late endosomes in non-polarised cells.
Authors:
Alicia Cabezas; Kristi G Bache; Andreas Brech; Harald Stenmark
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-05-24
Journal Detail:
Title:  Journal of cell science     Volume:  118     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-06-09     Completed Date:  2005-10-27     Revised Date:  2010-10-20    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2625-35     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, the Norwegian Radium Hospital, Montebello, Oslo.
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MeSH Terms
Descriptor/Qualifier:
Actins / chemistry,  genetics,  metabolism*
Antigens, CD / metabolism
Calcium-Binding Proteins / biosynthesis,  deficiency,  genetics,  metabolism*
Carrier Proteins / biosynthesis,  genetics,  metabolism*
Cell Cycle Proteins / biosynthesis,  genetics,  metabolism*
Cells, Cultured
Clathrin / chemistry,  metabolism
Cortactin
Down-Regulation
Endocytosis
Endosomal Sorting Complexes Required for Transport
Endosomes / chemistry,  metabolism*,  ultrastructure
Hela Cells
Humans
Intracellular Membranes
Lysophospholipids / metabolism
Microfilament Proteins / metabolism
Monoglycerides
Platelet Membrane Glycoproteins / metabolism
Protein Binding
Protein Transport
RNA, Small Interfering / genetics,  metabolism
Receptor, Epidermal Growth Factor / metabolism
Transferrin / metabolism
rab GTP-Binding Proteins / metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Antigens, CD; 0/CD63 antigen; 0/CTTN protein, human; 0/Calcium-Binding Proteins; 0/Carrier Proteins; 0/Cell Cycle Proteins; 0/Clathrin; 0/Cortactin; 0/Endosomal Sorting Complexes Required for Transport; 0/Lysophospholipids; 0/Microfilament Proteins; 0/Monoglycerides; 0/PDCD6IP protein, human; 0/Platelet Membrane Glycoproteins; 0/RNA, Small Interfering; 0/bis(monoacylglyceryl)phosphate; 11096-37-0/Transferrin; EC 2.7.10.1/Receptor, Epidermal Growth Factor; EC 3.6.1.-/rab GTP-Binding Proteins; EC 3.6.1.-/rab11 protein

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


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