Abstract
The actin binding proteins cortexillin I and II play a major role in Dictyostelium cytokinesis, in which they are found localized to the membranes of the cleavage furrow. Here we report on cortexillin I mutants isolated by gene trapping in Polysphondylium. The original mutation and reconstructed versions of the original, as well as cortexillin I deletions, are unable to form aggregation streams under starvation conditions. The fruiting bodies that do form when cells are grown on bacterial lawns lack the one- and two-dimensional symmetries so apparent in wild type. These two phenotypes and the proposed structural basis for them suggest that cortexillin I functions in chemotaxis and morphogenesis in addition to its role in cytokinesis.
Copyright 1999 Academic Press.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Bridged Bicyclo Compounds, Heterocyclic
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Cell Division / physiology
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Chemotaxis
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Cloning, Molecular
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Cytoskeleton / physiology
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Dimerization
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Gene Dosage
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Gene Expression Regulation, Developmental
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Molecular Sequence Data
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Morphogenesis
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Mutation
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Myxomycetes / growth & development*
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Polymerase Chain Reaction
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Protozoan Proteins
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Sequence Homology, Amino Acid
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Thiazoles
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Thiazolidines
Substances
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Bridged Bicyclo Compounds, Heterocyclic
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Microfilament Proteins
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Protein Isoforms
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Protozoan Proteins
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Thiazoles
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Thiazolidines
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ctxA protein, Dictyostelium discoideum
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ctxB protein, Dictyostelium discoideum
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latrunculin A
Associated data
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GENBANK/AF151101
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GENBANK/AF151102