Document Detail


Retargeting of the mitochondrial protein p32/gC1Qr to a cytoplasmic compartment and the cell surface.
MedLine Citation:
PMID:  11493647     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
p32/gC1qR is a small acidic protein that has been reported to have a broad range of distinct functions and to associate with a wide array of cellular, viral and bacterial proteins. It has been found in each of the main cellular compartments including mitochondria, nucleus and cytoplasm and is also thought to be located at the plasma membrane and secreted into the extracellular matrix. The true physiological role(s) of p32 remains controversial because it has been difficult to reconcile all of the findings on protein interactions and the seemingly disparate observations on compartmentalisation. However, it has been proposed that p32 is somehow involved in transport processes connecting diverse cellular compartments and the cell surface. Here we show that native p32 appears to be localised mainly in the mitochondria and is not detectable on the cell surface. However, addition of a short tag to the N-terminus of p32 appears to block its mitochondrial targeting, resulting in redirection into a cytoplasmic vesicular pattern, overlapping with the endoplasmic reticulum. The redirection of p32 results in an alteration in and co-localisation with ER markers including calreticulin, a lumenal ER chaperone. Furthermore, we show both by immunofluorescence and cross-linking studies that this also results in cell-surface expression of p32. These results indicate that, at least under certain circumstances, p32 can be retargeted and may help to provide an explanation for the diverse observations on its localization.
Authors:
H C van Leeuwen; P O'Hare
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cell science     Volume:  114     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2001 Jun 
Date Detail:
Created Date:  2001-08-08     Completed Date:  2001-12-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  2115-23     Citation Subset:  IM    
Affiliation:
Marie Curie Research Institute, The Chart, Oxted, Surrey, RH8 0TL, UK.
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MeSH Terms
Descriptor/Qualifier:
Adaptor Protein Complex gamma Subunits
Animals
Biotinylation
COS Cells
Calcium-Binding Proteins / metabolism
Calnexin
Calreticulin
Cell Membrane / metabolism*
Cytoplasm / metabolism*
Endoplasmic Reticulum / metabolism
Fluorescent Antibody Technique
Membrane Glycoproteins*
Membrane Proteins / metabolism
Mitochondria / metabolism*
Protein Transport
Receptors, Complement / chemistry,  genetics,  metabolism*
Recombinant Fusion Proteins / chemistry,  metabolism
Ribonucleoproteins / metabolism
Chemical
Reg. No./Substance:
0/Adaptor Protein Complex gamma Subunits; 0/Calcium-Binding Proteins; 0/Calreticulin; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Receptors, Complement; 0/Recombinant Fusion Proteins; 0/Ribonucleoproteins; 0/complement 1q receptor; 139873-08-8/Calnexin

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


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