Document Detail

Identification, localization, and functional implications of the microdomain-forming stomatin family in the ciliated protozoan Paramecium tetraurelia.
MedLine Citation:
PMID:  23376944     Owner:  NLM     Status:  MEDLINE    
The SPFH protein superfamily is assumed to occur universally in eukaryotes, but information from protozoa is scarce. In the Paramecium genome, we found only Stomatins, 20 paralogs grouped in 8 families, STO1 to STO8. According to cDNA analysis, all are expressed, and molecular modeling shows the typical SPFH domain structure for all subgroups. For further analysis we used family-specific sequences for fluorescence and immunogold labeling, gene silencing, and functional tests. With all family members tested, we found a patchy localization at/near the cell surface and on vesicles. The Sto1p and Sto4p families are also associated with the contractile vacuole complex. Sto4p also makes puncta on some food vacuoles and is abundant on vesicles recycling from the release site of spent food vacuoles to the site of nascent food vacuole formation. Silencing of the STO1 family reduces mechanosensitivity (ciliary reversal upon touching an obstacle), thus suggesting relevance for positioning of mechanosensitive channels in the plasmalemma. Silencing of STO4 members increases pulsation frequency of the contractile vacuole complex and reduces phagocytotic activity of Paramecium cells. In summary, Sto1p and Sto4p members seem to be involved in positioning specific superficial and intracellular microdomain-based membrane components whose functions may depend on mechanosensation (extracellular stimuli and internal osmotic pressure).
Alexander T Reuter; Claudia A O Stuermer; Helmut Plattner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-02-02
Journal Detail:
Title:  Eukaryotic cell     Volume:  12     ISSN:  1535-9786     ISO Abbreviation:  Eukaryotic Cell     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-29     Completed Date:  2013-09-13     Revised Date:  2013-10-08    
Medline Journal Info:
Nlm Unique ID:  101130731     Medline TA:  Eukaryot Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  529-44     Citation Subset:  IM    
Department of Biology, University of Konstanz, Konstanz, Germany.
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MeSH Terms
Cell Membrane / chemistry,  physiology*
Gene Expression Regulation
Gene Silencing
Genome, Protozoan*
Mechanotransduction, Cellular / physiology
Membrane Microdomains / chemistry,  physiology*
Membrane Proteins / genetics,  metabolism*
Multigene Family
Paramecium tetraurelia / chemistry,  physiology*
Phagocytosis / physiology
Phagosomes / chemistry,  physiology
Protein Structure, Tertiary
Transport Vesicles / chemistry,  physiology*
Vacuoles / chemistry,  physiology
Reg. No./Substance:
0/Membrane Proteins

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

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