| pubmed-article:12455698 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C0024501 | lld:lifeskim |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C0243040 | lld:lifeskim |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C1260875 | lld:lifeskim |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C1947912 | lld:lifeskim |
| pubmed-article:12455698 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:12455698 | pubmed:dateCreated | 2002-11-28 | lld:pubmed |
| pubmed-article:12455698 | pubmed:abstractText | Fungal adhesins represent a large family of serine/threonine-rich secreted glycoproteins. Adhesins have been shown to play roles in heterotypic and homotypic cell-cell adhesion processes, morphogenetic pathways and invasive/pseudohyphal growth, frequently in response to differentiation cues. Here we address the role of the Saccharomyces cerevisiae mating-specific adhesin Fig2p. Cells lacking FIG2 possess a variety of mating defects that relate to processes involving the cell wall, including morphogenetic defects, cell fusion defects, and alterations in agglutination activities. We found that mating-specific morphogenetic defects caused by the absence of FIG2 are suppressible by increased external osmolarity and that, during mating, fig2delta cells display reduced viability relative to wild-type cells. These defects result from alterations in signaling activated by the mating and cell integrity pathways. Finally, we show that fig2delta zygotes also have defects in zygotic spindle positioning that are osmoremedial, whereas the requirements for FIG2 in normal cell-cell agglutination and cell fusion during mating are insensitive to changes in the extracellular osmotic environment. We conclude that FIG2 performs distinct functions in the mating cell wall that are separable with respect to their ability to be suppressed by changes in external osmolarity and that a fundamental role of FIG2 in mating cells is the maintenance of cell integrity. | lld:pubmed |
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| pubmed-article:12455698 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12455698 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12455698 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12455698 | pubmed:author | pubmed-author:ZhangMinglian... | lld:pubmed |
| pubmed-article:12455698 | pubmed:author | pubmed-author:BennettDaniel... | lld:pubmed |
| pubmed-article:12455698 | pubmed:author | pubmed-author:ErdmanScott... | lld:pubmed |
| pubmed-article:12455698 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12455698 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12455698 | pubmed:pagination | 811-22 | lld:pubmed |
| pubmed-article:12455698 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12455698 | pubmed:articleTitle | Maintenance of mating cell integrity requires the adhesin Fig2p. | lld:pubmed |
| pubmed-article:12455698 | pubmed:affiliation | Department of Biology, Syracuse University, Syracuse, New York 13244-1220, USA. | lld:pubmed |
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