Proteomics

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Cellular concentrations of Protein Kinase D1 in HEK293T and INS-1 cells

ABSTRACT: Protein kinase D1 (PRKD1, also referred to as PKD1), has been proposed to undergo concentration dependent dimerization in vitro. To test whether the cellular concentration of PKD1 is in the range of the dissociation constant obtained, the expression level of PKD1 was investigated by PRM. To this end, an equimolar mixture of pure, recombinant protein comprising the PKD N-terminus (residues 48-198) and C-terminus (residues 395-892) was used to spike the cell lysates of human HEK293T cells or the rat cell line INS-1. In the latter case, only peptides that are identical between the human and rat PKD1 protein were used to estimate the cellular expression level of PKD1.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive HF

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human)

SUBMITTER: Markus Hartl  

LAB HEAD: Thomas A. Leonard

PROVIDER: PXD013232 | Pride | 2019-08-19

REPOSITORIES: Pride

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Dataset's files

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Action DRS
20180322_QexHF1_RSLC1_Elsner_Leonard_MFPL_PRM_1.raw Raw
20180322_QexHF1_RSLC1_Elsner_Leonard_MFPL_PRM_2_spiked_500ng.raw Raw
20180322_QexHF1_RSLC1_Elsner_Leonard_MFPL_PRM_3_spiked_50ng.raw Raw
20180322_QexHF1_RSLC1_Elsner_Leonard_MFPL_PRM_4_spiked_5ng.raw Raw
20180611_QexHF1_RSLC1_Elsner_Leonard_MFPL_PRM_500ng.raw Raw
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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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