Dataset Information

Plasmodium falciparum PfPK7-Dependent Phosphoproteome

ABSTRACT: In this project we use MS2-based 6-plex TMT quantitation to compare phosphorylation site abundances across several stages of the Plasmodium falciparum life cycle in wild-type Plasmodium and in a strain whose PK7 has been knocked out. See Pease et al. (2018) J. Proteome Res. for details.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Plasmodium Falciparum Homo Sapiens (human)

DISEASE(S): Malaria

SUBMITTER: Edward Huttlin

LAB HEAD: Steven P. Gygi

PROVIDER: PXD009465 | Pride | 2018-10-04

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	86605_t04175_EH_Malaria_Phos_SCX1_out.tgz	Other
	86606_t04176_EH_Malaria_Phos_SCX2_out.tgz	Other
	86607_t04177_EH_Malaria_Phos_SCX3_out.tgz	Other
	86608_t04178_EH_Malaria_Phos_SCX4_out.tgz	Other
	86609_t04179_EH_Malaria_Phos_SCX5_out.tgz	Other

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Publications

Characterization of Plasmodium falciparum Atypical Kinase PfPK7<sup>-</sup> Dependent Phosphoproteome.

Pease Brittany N BN Huttlin Edward L EL Jedrychowski Mark P MP Dorin-Semblat Dominique D Sebastiani Daniela D Segarra Daniel T DT Roberts Bracken F BF Chakrabarti Ratna R Doerig Christian C Gygi Steven P SP Chakrabarti Debopam D

Journal of proteome research 20180430 6

PfPK7 is an "orphan" kinase displaying regions of homology to multiple protein kinase families. PfPK7 functions in regulating parasite proliferation/development as evident from the phenotype analysis of knockout parasites. Despite this regulatory role, the functions of PfPK7 in signaling pathways are not known. To better understand PfPK7-regulated phosphorylation events, we performed isobaric tag-based quantitative comparative phosphoproteomics of the schizont and segmenter stages from wild-type ...[more]

PMID: 29678115

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Project description:Quantitative studies of the P. falciparum transcriptome have shown that the tightly controlled progression of the parasite through the intraerythrocytic developmental cycle (IDC) is accompanied by a continuous gene expression cascade where most expressed genes exhibit a single transcriptional peak. Since proteins represent the decisive business end of gene expression, understanding the correlation between mRNA and protein levels is crucial for inferring biological activity from transcriptional gene expression data. While pertinent studies on other organisms show that as little as 20-40% of protein abundance variation may be attributable to corresponding mRNA levels, the situation in Plasmodium is further complicated by the dynamic nature of the cyclic gene expression cascade where the mRNA levels of most genes change constantly during the IDC. In this study, we simultaneously determined mRNA and protein abundance profiles for P. falciparum parasites during the IDC at 2-hour resolution based on spotted oligonucleotide microarrays and 2D-protein gels in combination with DIGE fluorescent dyes. Intriguingly, most proteins are represented by more than one isoform, presumably due to post-translational modifications. Analysis of 366 protein abundance profiles and the corresponding mRNA levels shows that in 67.2% of cases the protein abundance peaks at least 8 hours after the mRNA level peak. While it may be tempting to interpret this as evidence for widespread post-transcriptional gene regulation additional analyses including computer modeling demonstrate that in >60% of these cases the observed protein profiles including the peak lag times could arise as a consequence of the corresponding mRNA levels when simple translation and degradation dynamics are assumed. We further characterize and illustrate these dynamics and show that even human host proteins within the parasite may be subject to similar dynamics as their parasite counterparts. 24 timepoint samples were harvested from a tightly synchronous 6.5 liter biofermenter culture of P. falciparum (Dd2) at 2-hour intervals during one entire intraerythrocytic developmental cycle and compared against a 3D7 RNA reference pool.