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Regulation of 3-phosphoinositide-dependent protein kinase 1 activity by homodimerization in live cells.

Science signaling - 26 Oct 2010

Masters Thomas A, Calleja Véronique, Armoogum Daven A, Marsh Richard J, Applebee Christopher J, Laguerre Michel, Bain Angus J, Larijani Banafshé

Abstract excerpt

3-Phosphoinositide-dependent kinase 1 (PDK1) plays a central role in regulating the activity of protein kinases that are essential for signaling; however, how PDK1 itself is regulated is largely unknown. We found that homodimerization of PDK1 is a spatially and temporally regulated mechanism for controlling PDK1 activity. We used Förster resonance energy transfer monitored by fluorescence lifetime imaging...

Topics

3-Phosphoinositide-Dependent Protein Kinases
Animals
COS Cells
Chlorocebus aethiops
Enzyme Activation
Fluorescence Resonance Energy Transfer
Humans
Mice
Mutation
NIH 3T3 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinase Inhibitors

Protein Multimerization

Protein Serine-Threonine Kinases

Protein Structure, Tertiary

Source

Identifiers

PMID: 20978239
DOI: 10.1126/scisignal.2000738

Genes

PDK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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