Document Detail


Asymmetric localization of flotillins/reggies in preassembled platforms confers inherent polarity to hematopoietic cells.
MedLine Citation:
PMID:  12826615     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hematopoietic cells have long been defined as round, nonpolar cells that show uniform distribution of cell surface-associated molecules. However, recent analyses of the immunological synapse and the importance of lipid microdomains in signaling have shed new light on the aspect of lymphocyte polarization during the activation processes, but none of the molecules implicated so far in either the activation process or the microdomain residency are known to have a preferential localization in nonactivated cells. Chemical crosslinking and fluorescence resonance energy transfer methods have allowed the visualization of certain glycosylphosphatidylinositol-anchored proteins in lipid rafts but so far no microdomain resident protein has been shown to exist as visible stable platforms in the membrane. We report here that two lipid microdomain resident proteins, flotillins/reggies, form preassembled platforms in hematopoietic cells. These platforms recruit signaling molecules upon activation through lipid rafts. The preassembled platforms significantly differ from the canonical cholesterol-dependent "lipid rafts," as they are resistant to cholesterol-disrupting agents. Most evidence for the functional relevance of microdomains in living cells remains indirect. Using laser scanning confocal microscopy, we show that these proteins exist as stable, microscopically patent domains localizing asymmetrically to one pole of the cell. We present evidence that the asymmetric concentration of these microdomain resident proteins is built up during cytokinesis.
Authors:
Lawrence Rajendran; Madhan Masilamani; Samuel Solomon; Ritva Tikkanen; Claudia A O Stuermer; Helmut Plattner; Harald Illges
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2003-06-25
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  100     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2003 Jul 
Date Detail:
Created Date:  2003-07-09     Completed Date:  2003-09-04     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8241-6     Citation Subset:  IM    
Affiliation:
Division of Immunology, Department of Biology, University of Konstanz, 78457 Konstanz, Germany.
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MeSH Terms
Descriptor/Qualifier:
Antigens, CD / analysis
B-Lymphocytes / metabolism,  ultrastructure*
Cell Division
Cell Polarity / physiology*
Cholera Toxin / pharmacology
Cholesterol / analysis
Cyclodextrins / pharmacology
Detergents / pharmacology
Green Fluorescent Proteins
Humans
Ionophores / pharmacology
Jurkat Cells / metabolism,  ultrastructure
Luminescent Proteins / analysis
Lymphocyte Activation / physiology*
Membrane Lipids / analysis
Membrane Microdomains / chemistry,  drug effects,  physiology*
Membrane Proteins / analysis,  physiology*
Nocodazole / pharmacology
Octoxynol / pharmacology
Recombinant Fusion Proteins / analysis
T-Lymphocytes / metabolism,  ultrastructure*
Tetradecanoylphorbol Acetate / pharmacology
Tumor Cells, Cultured / metabolism,  ultrastructure
beta-Cyclodextrins*
Chemical
Reg. No./Substance:
0/Antigens, CD; 0/Cyclodextrins; 0/Detergents; 0/Ionophores; 0/Luminescent Proteins; 0/Membrane Lipids; 0/Membrane Proteins; 0/Recombinant Fusion Proteins; 0/beta-Cyclodextrins; 0/flotillins; 0/methyl-beta-cyclodextrin; 147336-22-9/Green Fluorescent Proteins; 16561-29-8/Tetradecanoylphorbol Acetate; 31430-18-9/Nocodazole; 57-88-5/Cholesterol; 9002-93-1/Octoxynol; 9012-63-9/Cholera Toxin
Comments/Corrections

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