Document Detail

A novel Dictyostelium cell surface protein important for both cell adhesion and cell sorting.
MedLine Citation:
PMID:  9693138     Owner:  NLM     Status:  MEDLINE    
A mutant of Dictyostelium that is aberrant in the process of tip formation (dtfA-: defective in tip formation A) has been isolated by gene tagging. The dtfA gene is predicted to encode a protein of 163 kDa. There are no extensive sequence homologies between DTFA and previously identified proteins, but four short N-terminal sequence motifs show partial homology to repeats found in mammalian mucins. Immunofluorescence reveals a lattice-like arrangement of DTFA protein at the cell surface. When developing on a bacterial lawn, cells of the mutant strain (dtfA- cells) aggregate to form tight mounds, but development then becomes arrested. When developed in the absence of nutrients, a fraction of dtfA- cells complete development, but there is a long delay at the tight mound stage and the culminants that eventually form are aberrant. In such dtfA- mounds the prestalk cells fail to move to the apex on cue and so tip formation is delayed. dtfA- cells also show a conditional defect in early development, in that they are unable to aggregate when plated at low density. In addition dtfA- cells do not agglomerate efficiently when shaken in suspension. In combination, these results suggest that DTFA may form part of a cell-cell adhesion system that is needed both for optimal aggregation and for efficient cell sorting during multicellular development. The DTFA protein also appears to be important during cell growth, because cytokinesis is defective and the actin cytoskeleton aberrant in growing dtfA- cells.
R S Ginger; L Drury; C Baader; N V Zhukovskaya; J G Williams
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Development (Cambridge, England)     Volume:  125     ISSN:  0950-1991     ISO Abbreviation:  Development     Publication Date:  1998 Sep 
Date Detail:
Created Date:  1998-10-14     Completed Date:  1998-10-14     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  8701744     Medline TA:  Development     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  3343-52     Citation Subset:  IM    
MRC Laboratory of Molecular Cell Biology and Department of Biology, University College London, Gower Street, London WC1E 6BT, UK.
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MeSH Terms
Amino Acid Sequence
Cell Adhesion / genetics,  physiology
Cell Division / genetics,  physiology
Chemotaxis / genetics,  physiology
Dictyostelium / cytology*,  genetics,  physiology*
Fungal Proteins / genetics,  physiology*
Genes, Fungal
Genes, Protozoan
Membrane Proteins / genetics,  physiology*
Molecular Sequence Data
Mucins / genetics
Protozoan Proteins / genetics,  physiology*
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Fungal Proteins; 0/Membrane Proteins; 0/Mucins; 0/Protozoan Proteins; 0/dftA protein, Dictyostelium discoideum

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