| Association of a GPI-anchored protein with detergent-resistant membranes facilitates its trafficking through the early secretory pathway. | |
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MedLine Citation:
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PMID: 19022244 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Zeynep Hein; Nigel M Hooper; Hassan Y Naim |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-11-07 |
Journal Detail:
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Title: Experimental cell research Volume: 315 ISSN: 1090-2422 ISO Abbreviation: Exp. Cell Res. Publication Date: 2009 Jan |
Date Detail:
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Created Date: 2008-12-29 Completed Date: 2009-02-11 Revised Date: 2012-07-04 |
Medline Journal Info:
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Nlm Unique ID: 0373226 Medline TA: Exp Cell Res Country: United States |
Other Details:
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Languages: eng Pagination: 348-56 Citation Subset: IM |
Affiliation:
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Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Bünteweg 17, D-30559 Hannover, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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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