Document Detail

Ndm, a coiled-coil domain protein that suppresses macropinocytosis and has effects on cell migration.
MedLine Citation:
PMID:  22809629     Owner:  NLM     Status:  MEDLINE    
The ampA gene has a role in cell migration in Dictyostelium discoideum. Cells overexpressing AmpA show an increase in cell migration, forming large plaques on bacterial lawns. A second-site suppressor of this ampA-overexpressing phenotype identified a previously uncharacterized gene, ndm, which is described here. The Ndm protein is predicted to contain a coiled-coil BAR-like domain-a domain involved in endocytosis and membrane bending. ndm-knockout and Ndm-monomeric red fluorescent protein-expressing cell lines were used to establish a role for ndm in suppressing endocytosis. An increase in the rate of endocytosis and in the number of endosomes was detected in ndm(-) cells. During migration ndm(-) cells formed numerous endocytic cups instead of the broad lamellipodia structure characteristic of moving cells. A second lamellipodia-based function-cell spreading-was also defective in the ndm(-) cells. The increase in endocytosis and the defect in lamellipodia formation were associated with reduced chemotaxis in ndm(-) cells. Immunofluorescence results and glutathione S-transferase pull-down assays revealed an association of Ndm with coronin and F-actin. The results establish ndm as a gene important in regulating the balance between formation of endocytic cups and lamellipodia structures.
Jessica S Kelsey; Nathan M Fastman; Elizabeth F Noratel; Daphne D Blumberg
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-07-18
Journal Detail:
Title:  Molecular biology of the cell     Volume:  23     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-08-31     Completed Date:  2013-02-22     Revised Date:  2013-07-12    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3407-19     Citation Subset:  IM    
Department of Biological Sciences, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
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MeSH Terms
4-Butyrolactone / analogs & derivatives,  metabolism
Actin Cytoskeleton / ultrastructure
Actins / metabolism
Cell Line
Cell Movement*
Dictyostelium / genetics,  metabolism,  physiology*,  ultrastructure
Gene Knockout Techniques
Metalloendopeptidases / genetics,  metabolism
Protein Structure, Tertiary
Protozoan Proteins / chemistry*,  genetics,  metabolism*
Pseudopodia / metabolism,  ultrastructure
Reg. No./Substance:
0/Actins; 0/Protozoan Proteins; 0/coronin; 96-48-0/4-Butyrolactone; EC 3.4.24.-/AmpA protein, Dictyostelium protozoan; EC 3.4.24.-/Metalloendopeptidases

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