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PMID:24281718

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Citation

Douglas, LM, Wang, HX and Konopka, JB (2013) The MARVEL domain protein Nce102 regulates actin organization and invasive growth of Candida albicans. MBio 4:e00723-13

Abstract

Invasive growth of the fungal pathogen Candida albicans into tissues promotes disseminated infections in humans. The plasma membrane is essential for pathogenesis because this important barrier mediates morphogenesis and invasive growth, as well as secretion of virulence factors, cell wall synthesis, nutrient import, and other processes. Previous studies showed that the Sur7 tetraspan protein that localizes to MCC (membrane compartment occupied by Can1)/eisosome subdomains of the plasma membrane regulates a broad range of key functions, including cell wall synthesis, morphogenesis, and resistance to copper. Therefore, a distinct tetraspan protein found in MCC/eisosomes, Nce102, was investigated. Nce102 belongs to the MARVEL domain protein family, which is implicated in regulating membrane structure and function. Deletion of NCE102 did not cause the broad defects seen in sur7Δ cells. Instead, the nce102Δ mutant displayed a unique phenotype in that it was defective in forming hyphae and invading low concentrations of agar but could invade well in higher agar concentrations. This phenotype was likely due to a defect in actin organization that was observed by phalloidin staining. In support of this, the invasive growth defect of a bni1Δ mutant that mislocalizes actin due to lack of the Bni1 formin was also reversed at high agar concentrations. This suggests that a denser matrix provides a signal that compensates for the actin defects. The nce102Δ mutant displayed decreased virulence and formed abnormal hyphae in mice. These studies identify novel ways that Nce102 and the physical environment surrounding C. albicans regulate morphogenesis and pathogenesis.

Links

PubMed PMC3870249 Online version:10.1128/mBio.00723-13

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

CANAL:NCE2

acts_upstream_of_or_within

GO:0030036: actin cytoskeleton organization

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

CANAL:NCE2

located_in

GO:0032126: eisosome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

CANAL:NCE2

GO:0007015: actin filament organization

ECO:0000315:

P

Figure 7a shows that in comparison with the wild type, a mutated Nce102 gene causes actin mislocalization. Fig 7b shows that the cells were also more round that the wild type which can indicate an actin defect

complete
CACAO 9675

CANAL:NCE2

involved_in

GO:0030036: actin cytoskeleton organization

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

CANAL:NCE2

part_of

GO:0032126: eisosome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

CANAL:NCE2

involved_in

GO:0007015: actin filament organization

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

CANAL:NCE2

involved_in

GO:0009405: pathogenesis

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

See also

References

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