Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

Capturing conformational transitions of full-length PDK1 that dictate kinase substrate selectivity

PDK1 is a constitutively active master kinase that can phosphorylate and activate as many as 24 enzymes, all belonging to the AGC family of serine-threonine protein kinases. In this issue of , Sacerdoti . uncover how allosteric communication between different functional domains directs the selectivi...

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Veröffentlicht in:Science signaling 2023-06, Vol.16 (789), p.eadh5114-eadh5114
Hauptverfasser: Martínez-Arenas, Laura, Bayascas, Jose R
Format: Artikel
Sprache:eng
Schlagworte:
Kinases
Protein Serine-Threonine Kinases - genetics
Signal Transduction
Substrates
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Zusammenfassung:PDK1 is a constitutively active master kinase that can phosphorylate and activate as many as 24 enzymes, all belonging to the AGC family of serine-threonine protein kinases. In this issue of , Sacerdoti . uncover how allosteric communication between different functional domains directs the selectivity of PDK1 toward particular subsets of substrates.
ISSN:1945-0877
1937-9145
DOI:10.1126/scisignal.adh5114