Proteomics

Dataset Information

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Analysis of PKD1 autophosphorylation in vitro and confirmation of stoichiometric S742 phosphorylation of a recombinant PRKD1 kinase domain

ABSTRACT: Protein kinase D1 (PRKD1, also referred to as PKD1), has been proposed to undergo autophosphorylation on serine 742 and potentially also on serine 738 in the activation loop of its kinase domain. We used recombinant PKD1 kinase domain to test whether PKD1 is indeed able to undergo autophosphorylation of its kinase domain and how many sites could be phosphorylated. In order to obtain fully phosphorylated PKD1 kinase domain we adapted our autophosphorylation protocol to obtain monophosphorylated PKD1 kinase domain and determined the phosphorylation site by ArgC digest and phosphopeptide mapping.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Markus Hartl  

LAB HEAD: Thomas A. Leonard

PROVIDER: PXD013216 | Pride | 2019-08-19

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20170130_QexHF2_RSLC2_Elsner_Leonard_MFPL_insol_PDK_ArgC_50p.raw Raw
20170927_QexHF4_RSLC4_Elsner_Leonard_MFPL_insol_PKDCAT12_ArgC_10p.raw Raw
2018.08_uniprot-taxonomy3A7106_allSpodoptera.fasta Fasta
2019.01_UP000005204_7091_Bombyx_mori_all.fasta Fasta
MaxQuant_1.6.0.16.zip Other
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Publications

A ubiquitin-like domain controls protein kinase D dimerization and activation by trans-autophosphorylation.

Elsner Daniel J DJ   Siess Katharina M KM   Gossenreiter Thomas T   Hartl Markus M   Leonard Thomas A TA  

The Journal of biological chemistry 20190812 39

Protein kinase D (PKD) is an essential Ser/Thr kinase in animals and controls a variety of diverse cellular functions, including vesicle trafficking and mitogenesis. PKD is activated by recruitment to membranes containing the lipid second messenger diacylglycerol (DAG) and subsequent phosphorylation of its activation loop. Here, we report the crystal structure of the PKD N terminus at 2.2 Å resolution containing a previously unannotated ubiquitin-like domain (ULD), which serves as a dimerization  ...[more]

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