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Cross-link mass spectrometry reveals conformational changes within the N lobe and the activation loop of PDK1 upon dimerization

ABSTRACT: Cross-linking mass spectrometry analysis of the PDK1 kinase domain dimer that undergoes trans-autophosphorylation.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dorothea Anrather

LAB HEAD: Thomas A. Leonard

PROVIDER: PXD031827 | Pride | 2022-05-20

REPOSITORIES: Pride

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			Action	DRS
	20191213_Lumos_RSLC6_Levina_Leonard_MFPL_PDK1_XL_EDC_Dimer_20p.raw	Raw
	20191213_Lumos_RSLC6_Levina_Leonard_MFPL_PDK1_XL_EDC_Monomer_20p.raw	Raw
	20211209_QExHFX2_RSLC10_Levina_Leonard_MPL_MUW_XL_dimer_30p.raw	Raw
	20211209_QExHFX2_RSLC10_Levina_Leonard_MPL_MUW_XL_monomer_2p.raw	Raw
	BS3_MQ_txt.zip	Other

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Publications

Activation of the essential kinase PDK1 by phosphoinositide-driven trans-autophosphorylation.

Levina Aleksandra A Fleming Kaelin D KD Burke John E JE Leonard Thomas A TA

Nature communications 20220406 1

3-phosphoinositide-dependent kinase 1 (PDK1) is an essential serine/threonine protein kinase, which plays a crucial role in cell growth and proliferation. It is often referred to as a 'master' kinase due to its ability to activate at least 23 downstream protein kinases implicated in various signaling pathways. In this study, we have elucidated the mechanism of phosphoinositide-driven PDK1 auto-activation. We show that PDK1 trans-autophosphorylation is mediated by a PIP<sub>3</sub>-mediated face- ...[more]

PMID: 35387990

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