Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development

ABSTRACT Among the hemiascomycetes, only Candida albicans must switch from the white phenotype to the opaque phenotype to mate. In the recent evolution of this transition, mating-incompetent white cells acquired a unique response to mating pheromone, resulting in the formation of a white cell biofil...

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Autores principales:	Song Yi, Nidhi Sahni, Karla J. Daniels, Kevin L. Lu, Guanghua Huang, Adam M. Garnaas, Claude Pujol, Thyagarajan Srikantha, David R. Soll
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Lenguaje:	EN
Publicado:	American Society for Microbiology 2011
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/85056c9e241942dab5632a0962cc872b
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spelling	oai:doaj.org-article:85056c9e241942dab5632a0962cc872b2021-11-15T15:38:46ZUtilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development10.1128/mBio.00237-102150-7511https://doaj.org/article/85056c9e241942dab5632a0962cc872b2011-03-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00237-10https://doaj.org/toc/2150-7511ABSTRACT Among the hemiascomycetes, only Candida albicans must switch from the white phenotype to the opaque phenotype to mate. In the recent evolution of this transition, mating-incompetent white cells acquired a unique response to mating pheromone, resulting in the formation of a white cell biofilm that facilitates mating. All of the upstream components of the white cell response pathway so far analyzed have been shown to be derived from the ancestral pathway involved in mating, except for the mitogen-activated protein (MAP) kinase scaffold protein, which had not been identified. Here, through binding and mutational studies, it is demonstrated that in both the opaque and the white cell pheromone responses, Cst5 is the scaffold protein, supporting the evolutionary scenario proposed. Although Cst5 plays the same role in tethering the MAP kinases as Ste5 does in Saccharomyces cerevisiae, Cst5 is approximately one-third the size and has only one rather than four phosphorylation sites involved in activation and cytoplasmic relocalization. IMPORTANCE Candida albicans must switch from white to opaque to mate. Opaque cells then release pheromone, which not only induces cells to mate but also in a unique fashion induces mating-incompetent white cells to form biofilms that facilitate opaque cell mating. All of the tested upstream components of the newly evolved white cell pheromone response pathway, from the receptor to the mitogen-activated protein (MAP) kinase cascade, are the same as those of the conserved opaque cell response pathway. One key element, however, remained unidentified, the scaffold protein for the kinase cascade. Here, we demonstrate that Cst5, a homolog of the Saccharomyces cerevisiae scaffold protein Ste5, functions as the scaffold protein in both the opaque and the white cell pheromone responses. Pheromone induces Cst5 phosphorylation, which is involved in activation and cytoplasmic localization of Cst5. However, Cst5 contains only one phosphorylation site, not four as in the S. cerevisiae ortholog Ste5. These results support the hypothesis that the entire upper portion of the newly evolved white cell pheromone response pathway is derived from the conserved pheromone response pathway in the mating process.Song YiNidhi SahniKarla J. DanielsKevin L. LuGuanghua HuangAdam M. GarnaasClaude PujolThyagarajan SrikanthaDavid R. SollAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 2, Iss 1 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Song Yi Nidhi Sahni Karla J. Daniels Kevin L. Lu Guanghua Huang Adam M. Garnaas Claude Pujol Thyagarajan Srikantha David R. Soll Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
description	ABSTRACT Among the hemiascomycetes, only Candida albicans must switch from the white phenotype to the opaque phenotype to mate. In the recent evolution of this transition, mating-incompetent white cells acquired a unique response to mating pheromone, resulting in the formation of a white cell biofilm that facilitates mating. All of the upstream components of the white cell response pathway so far analyzed have been shown to be derived from the ancestral pathway involved in mating, except for the mitogen-activated protein (MAP) kinase scaffold protein, which had not been identified. Here, through binding and mutational studies, it is demonstrated that in both the opaque and the white cell pheromone responses, Cst5 is the scaffold protein, supporting the evolutionary scenario proposed. Although Cst5 plays the same role in tethering the MAP kinases as Ste5 does in Saccharomyces cerevisiae, Cst5 is approximately one-third the size and has only one rather than four phosphorylation sites involved in activation and cytoplasmic relocalization. IMPORTANCE Candida albicans must switch from white to opaque to mate. Opaque cells then release pheromone, which not only induces cells to mate but also in a unique fashion induces mating-incompetent white cells to form biofilms that facilitate opaque cell mating. All of the tested upstream components of the newly evolved white cell pheromone response pathway, from the receptor to the mitogen-activated protein (MAP) kinase cascade, are the same as those of the conserved opaque cell response pathway. One key element, however, remained unidentified, the scaffold protein for the kinase cascade. Here, we demonstrate that Cst5, a homolog of the Saccharomyces cerevisiae scaffold protein Ste5, functions as the scaffold protein in both the opaque and the white cell pheromone responses. Pheromone induces Cst5 phosphorylation, which is involved in activation and cytoplasmic localization of Cst5. However, Cst5 contains only one phosphorylation site, not four as in the S. cerevisiae ortholog Ste5. These results support the hypothesis that the entire upper portion of the newly evolved white cell pheromone response pathway is derived from the conserved pheromone response pathway in the mating process.
format	article
author	Song Yi Nidhi Sahni Karla J. Daniels Kevin L. Lu Guanghua Huang Adam M. Garnaas Claude Pujol Thyagarajan Srikantha David R. Soll
author_facet	Song Yi Nidhi Sahni Karla J. Daniels Kevin L. Lu Guanghua Huang Adam M. Garnaas Claude Pujol Thyagarajan Srikantha David R. Soll
author_sort	Song Yi
title	Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
title_short	Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
title_full	Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
title_fullStr	Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
title_full_unstemmed	Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development
title_sort	utilization of the mating scaffold protein in the evolution of a new signal transduction pathway for biofilm development
publisher	American Society for Microbiology
publishDate	2011
url	https://doaj.org/article/85056c9e241942dab5632a0962cc872b
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Utilization of the Mating Scaffold Protein in the Evolution of a New Signal Transduction Pathway for Biofilm Development

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