Document Detail


Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation.
MedLine Citation:
PMID:  12370178     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Flotillins are lipid raft-associated proteins, which have been implicated in neuronal regeneration and insulin signaling. We now show that newly synthesized flotillin-1 reaches the plasma membrane via a Sar1-independent and brefeldin A-resistant targeting pathway. Consistent with post-translational membrane association of flotillin, protease sensitivity experiments suggest that flotillin-1 is not a transmembrane protein but is associated with the cytoplasmic face of the plasma membrane. The N terminus of flotillin contains a prohibitin-like domain (PHB), which shows homology to a number of proteins associated with raft domains including stomatin, podocin, and prohibitin. We show that the PHB domain of flotillin can efficiently target a heterologous protein, green fluorescent protein, to the plasma membrane. Another PHB-containing protein, stomatin, traffics to the plasma membrane via the conventional secretory pathway. Plasma membrane association of both full-length flotillin and the green fluorescent protein-tagged PHB domain of flotillin is dependent on palmitoylation and requires a conserved cysteine residue, Cys-34, in the PHB domain. The results identify a novel targeting mechanism for plasma membrane association of flotillin-1 involving a Golgi-independent trafficking pathway, the PHB domain, and palmitoylation.
Authors:
Isabel C Morrow; Shane Rea; Sally Martin; Ian A Prior; Rainer Prohaska; John F Hancock; David E James; Robert G Parton
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2002-10-04
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Dec 
Date Detail:
Created Date:  2002-12-09     Completed Date:  2003-01-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  48834-41     Citation Subset:  IM    
Affiliation:
Institute for Molecular Bioscience and Centre for Functional and Applied Genomics, University of Queensland, St. Lucia, Australia.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Brefeldin A / pharmacology
Cell Membrane / drug effects,  metabolism
Cells, Cultured
Cercopithecus aethiops
Cricetinae
Cytoplasm / metabolism
DNA Primers
Fish Proteins*
Golgi Apparatus / metabolism*
Membrane Proteins / chemistry,  metabolism*
Molecular Sequence Data
Nerve Tissue Proteins / chemistry,  metabolism*
Palmitic Acid / metabolism*
Protein Transport
Sequence Homology, Amino Acid
Vero Cells
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Fish Proteins; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/flotillins; 0/reggie-2 protein, Carassius auratus; 20350-15-6/Brefeldin A; 57-10-3/Palmitic Acid

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


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