Functional characterization of myosin I tail regions in Candida albicans.
The molecular motor myosin I is required for hyphal growth in the pathogenic yeast Candida albicans. Specific myosin I functions were investigated by a deletion analysis of five neck and tail regions. Hyphal formation requires both the TH1 region and the IQ motifs. The TH2 region is important for optimal hyphal growth. All of the regions, except for the SH3 and acidic (A) regions that were examined individually, were required for the localization of myosin I at the hyphal tip. Similarly, all of the domains were required for the association of myosin I with pelletable actin-bound complexes. Moreover, the hyphal tip localization of cortical actin patches, identified by both rhodamine-phalloidin staining and Arp3-green fluorescent protein signals, was dependent on myosin I. Double deletion of the A and SH3 domains depolarized the distribution of the cortical actin patches without affecting the ability of the mutant to form hyphae, suggesting that myosin I has distinct functions in these processes. Among the six myosin I tail domain mutants, the ability to form hyphae was strictly correlated with endocytosis. We propose that the uptake of cell wall remodeling enzymes and excess plasma membrane is critical for hyphal formation.
Genetics Group, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H3A 2B2, Canada. ursula.oberholzer@nrc.ca.
Ursula
U
Oberholzer
Tatiana L
TL
Iouk
David Y
DY
Thomas
Malcolm
M
Whiteway
D000199:Actins / Q000235:genetics / Q000378:metabolism; D020816:Amino Acid Motifs; D001483:Base Sequence; D002176:Candida albicans / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D004271:DNA, Fungal / Q000235:genetics; D004705:Endocytosis / Q000235:genetics / Q000502:physiology; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005800:Genes, Fungal; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D024461:Myosin Type I / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016366:Open Reading Frames; D010641:Phenotype; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion
D000199:Actins; D004271:DNA, Fungal; D005656:Fungal Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D024461:Myosin Type I