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PMID: 11694587 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Candida albicans Int1p interacts with the septin ring in yeast and hyphal cells.

Molecular biology of the cell ·Vol. 12 ·No. 11 ·2001-11-00 ·Pages 3538-49

Gale C, Gerami-Nejad M, McClellan M, Vandoninck S, Longtine MS, Berman J

Abstract

The ability to switch between yeast and hyphal morphologies is an important virulence factor for the opportunistic pathogen Candida albicans. Although the kinetics of appearance of the filamentous ring that forms at the incipient septum differ in yeast and cells forming hyphae (germ tubes) (), the molecular mechanisms that regulate this difference are not known. Int1p, a C. albicans gene product with similarity in its C terminus to Saccharomyces cerevisiae Bud4p, has a role in hyphal morphogenesis. Here we report that in S. cerevisiae, Int1p expression results in the growth of highly polarized cells with delocalized chitin and defects in cytokinesis and bud-site selection patterns, phenotypes that are also seen in S. cerevisiae septin mutant strains. Expression of high levels of Int1p in S. cerevisiae generated elaborate spiral-like structures at the periphery of the polarized cells that contained septins and Int1p. In addition, Int1p coimmunoprecipitated with the Cdc11p and Cdc12p septins, and Cdc12p is required for the establishment and maintenance of these Int1p/septin spirals. Although Swe1p kinase contributes to INT1-induced filamentous growth in S. cerevisiae, it is not required for the formation of ectopic Int1p/septin structures. In C. albicans, Int1p was important for the axial budding pattern and colocalized with Cdc3p septin in a ring at the mother-bud neck of yeast and pseudohyphal cells. Under conditions that induce hyphae, both Cdc3p and Int1p localized to a ring distal to the junction of the mother cell and germ tube. Thus, placement of the Int1p/septin ring with respect to the mother-daughter cell junction distinguishes yeast/pseudohyphal growth from hyphal growth in C. albicans.

MeSH Terms
Candida albicans/growth & development,metabolism Cell Adhesion Molecules/genetics,metabolism,physiology Cell Cycle Proteins/genetics,metabolism Cell Division Cyclin-Dependent Kinases/metabolism Cytoskeletal Proteins Fungal Proteins/metabolism Myosin Heavy Chains/metabolism Profilins Protein Kinases/metabolism Protein Serine-Threonine Kinases Protein-Tyrosine Kinases/metabolism Recombinant Fusion Proteins/genetics,metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins
Chemicals
CDC11 protein, S cerevisiae CDC12 protein, S cerevisiae CDC3 protein, S cerevisiae Cell Adhesion Molecules Cell Cycle Proteins Cytoskeletal Proteins Fungal Proteins Profilins Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins alphaINT1 protein, Candida albicans Protein Kinases SWE1 protein, S cerevisiae Protein-Tyrosine Kinases GIN4 protein, S cerevisiae HSL1 protein, S cerevisiae Protein Serine-Threonine Kinases Cyclin-Dependent Kinases Myosin Heavy Chains
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Gale C
Department of Pediatrics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Gerami-Nejad M
McClellan M
Vandoninck S
Longtine M S
Berman J
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2001-11-00
Pages
3538-49
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC60274
Subset
IM
Grants
NIAID NIH HHS · AI-01712-02 · United States
NIAID NIH HHS · AI-25827 · United States
NIAID NIH HHS · K08 AI001712 · United States
NICHD NIH HHS · P30 HD33692 · United States
Wellcome Trust · United Kingdom
NICHD NIH HHS · K12 HD033692 · United States
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