PXD003685

PXD003685 is an original dataset announced via ProteomeXchange.

Title	The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans
Description	Candida albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to the systemic disease candidiasis. Its ability to adopt various morphological forms, such as unicellular yeasts, filamentous pseudohyphae and hyphae, contributes to its ability to survive within the host. It has been suggested that the antioxidant glutathione is involved in the filamentation process. We investigated S-glutathionylation, the reversible binding of glutathione to proteins, and the functional consequences on C. albicans metabolic remodeling during the yeast-to-hyphae transition. Our work provided evidence for the specific glutathionylation of mitochondrial proteins involved in bioenergetics pathways in filamentous forms and a regulation of the main enzyme of the glyoxylate cycle, isocitrate lyase, by glutathionylation. Our proteomic data demonstrate that the binding of one glutathione molecule to isocitrate lyase in the hyphal forms leads to enzyme inactivation which was reversed by glutaredoxin treatment. We also assessed the effect of alternative carbon sources on glutathione levels and isocitrate lyase activity. Changes in nutrient availability led to morphological flexibility and was related to perturbations in glutathione levels and isocitrate lyase activity, confirming the key role of the maintenance of intracellular redox status in the adaptive metabolic strategy of the pathogen.
HostingRepository	PRIDE
AnnounceDate	2016-04-21
AnnouncementXML	Submission_2016-04-21_00:15:31.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Camille GARCIA
SpeciesList	scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationList	phosphorylated residue; monohydroxylated residue; acetylated residue; deamidated residue; L-cysteine glutathione disulfide
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2016-02-25 01:22:52	ID requested
⏵ 1	2016-04-21 00:15:33	announced

Gergondey R, Garcia C, Serre V, Camadro JM, Auch, è, re F, The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans. Biochim Biophys Acta, 1862(7):1309-23(2016) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: Candida albicans / filamentation/ glutathionylation/ isocitrate lyase / mitochondria

Jean-Michel Camadro
contact affiliation	Institut Jacques Monod
contact email	jean-michel.camadro@ijm.fr
lab head
Camille GARCIA
contact affiliation	Institut Jacques Monod
contact email	camille.garcia@ijm.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003685
     1. Label: PRIDE project
     2. Name: The adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans