Transcriptional control of dimorphism in Candida albicans

Curr Opin Microbiol. 2001 Dec;4(6):728-35. doi: 10.1016/s1369-5274(01)00275-2.


Candida albicans uses a network of multiple signaling pathways to control the yeast-->hypha transition. These include a mitogen-activated protein kinase pathway through Cph1, the cAMP-dependent protein kinase pathway via Efg1, a pH-responsive pathway through Rim101, the Tup1-mediated repression through Rfg1 and Nrg1, and pathways represented by transcription factors Cph2, Tec1 and Czf1. These pathways control the transcription of a common set of hypha-specific genes, many of which encode known virulence factors. The link between the signaling pathways and hyphal elongation is currently unknown, but there is evidence to suggest that Cdc42 likely plays a key role in hyphal morphogenesis. Unlike pseudohyphal growth in Saccharomyces cerevisiae, hyphal elongation is regulated independently of the cell cycle. Cellular differences between pseudohyphae and hyphae are further revealed by septin localization.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Bacterial Proteins*
  • Candida albicans / cytology
  • Candida albicans / growth & development
  • Candida albicans / physiology*
  • Cell Polarity
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • DNA-Binding Proteins / physiology
  • Fungal Proteins / physiology
  • Gene Expression Regulation, Fungal
  • Hyphae / physiology
  • Mitogen-Activated Protein Kinases / metabolism
  • Phenotype
  • Phytochrome / physiology
  • Repressor Proteins / physiology
  • Signal Transduction
  • Transcription Factors / physiology


  • Bacterial Proteins
  • CPH1 protein, Candida albicans
  • Cph2 protein, bacteria
  • DNA-Binding Proteins
  • Fungal Proteins
  • RFG1 protein, Candida albicans
  • Repressor Proteins
  • TEC1 protein, Candida albicans
  • Transcription Factors
  • Phytochrome
  • Cyclic AMP-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinases