Dataset Information

YCf1 Phosphorylation status detection using mass spect

ABSTRACT: The Purified YCF1 protein was subjected to mass-spect for phosphorylation detection.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Nitesh Kumar Khandelwal

LAB HEAD: Thomas M. Tomasiak

PROVIDER: PXD031330 | Pride | 2022-05-20

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	1Quantitation_Report_of_TT_3112287_PTM_Experiment.csv	Csv
	PTM_List_Report_of_TT_3112287_PTM_Experiment.csv	Csv
	Protein_Report_of_TT_3112287_PTM_Experiment.csv	Csv
	Quantitation_Report_of_TT_3112287_PTM_Experiment.csv	Csv
	TT_3112287_PTM_Experiment.sptm	Other

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Publications

The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation.

Khandelwal Nitesh Kumar NK Millan Cinthia R CR Zangari Samantha I SI Avila Samantha S Williams Dewight D Thaker Tarjani M TM Tomasiak Thomas M TM

Nature communications 20220311 1

Yeast Cadmium Factor 1 (Ycf1) sequesters heavy metals and glutathione into the vacuole to counter cell stress. Ycf1 belongs to the ATP binding cassette C-subfamily (ABCC) of transporters, many of which are regulated by phosphorylation on intrinsically-disordered domains. The regulatory mechanism of phosphorylation is still poorly understood. Here, we report two cryo-EM structures of Ycf1 at 3.4 Å and 4.0 Å resolution in inward-facing open conformations that capture previously unobserved ordered ...[more]

PMID: 35277487

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