Document Detail


Association of a GPI-anchored protein with detergent-resistant membranes facilitates its trafficking through the early secretory pathway.
MedLine Citation:
PMID:  19022244     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Membrane microdomains are implicated in the trafficking and sorting of several membrane proteins. In particular GPI-anchored proteins cluster into Triton X-100 resistant, cholesterol- and sphingolipid-rich membrane microdomains and are sorted to the apical membrane. A growing body of evidence has pointed to the existence of other types of microdomains that are insoluble in detergents, such as Lubrol WX and Tween-20. Here, we report on the role of detergent-resistant membranes formed at early stages in the biosynthesis of membrane dipeptidase (MDP), a GPI-anchored protein, on its trafficking and sorting. Pulse-chase experiments revealed a retarded maturation rate of the GPI-anchor deficient mutant (MDPDeltaGPI) as compared to the wild type protein (wtMDP). However, Golgi to cell surface delivery rate did not show a significant difference between the two variants. On the other hand, early biosynthetic forms of wtMDP were partially insoluble in Tween-20, while MDPDeltaGPI was completely soluble. The lack of association of MDPDeltaGPI with detergent-resistant membranes prior to maturation in the Golgi and the reduction in its trafficking rate strongly suggest the existence of an early trafficking control mechanisms for membrane proteins operating at a level between the endoplasmic reticulum and the cis-Golgi.
Authors:
Zeynep Hein; Nigel M Hooper; Hassan Y Naim
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-11-07
Journal Detail:
Title:  Experimental cell research     Volume:  315     ISSN:  1090-2422     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2008-12-29     Completed Date:  2009-02-11     Revised Date:  2012-07-04    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  348-56     Citation Subset:  IM    
Affiliation:
Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Bünteweg 17, D-30559 Hannover, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Autoantigens / metabolism
Brefeldin A / pharmacology
COS Cells
Cell Line
Cell Membrane / metabolism
Cercopithecus aethiops
Dipeptidases / genetics,  metabolism*
Dogs
Endoplasmic Reticulum / metabolism
Glycosylation
Glycosylphosphatidylinositols / physiology*
Golgi Apparatus / metabolism
Kinetics
Luminescent Proteins / genetics,  metabolism
Membrane Microdomains / chemistry,  metabolism*
Membrane Proteins / metabolism
Mutation
Protein Folding
Protein Transport / drug effects,  physiology
Signal Transduction / physiology*
Swine
Transport Vesicles / metabolism
Trypsin / metabolism
Chemical
Reg. No./Substance:
0/Autoantigens; 0/Glycosylphosphatidylinositols; 0/Golgin subfamily A member 2; 0/Luminescent Proteins; 0/Membrane Proteins; 0/flotillins; 0/fluorescent protein 583; 20350-15-6/Brefeldin A; EC 3.4.13.-/Dipeptidases; EC 3.4.13.18/dipeptidase; EC 3.4.21.4/Trypsin

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


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