Assembly of allosteric macromolecular switches: Lessons from PKA

Susan S. Taylor, Ronit Ilouz, Ping Zhang, Alexandr P. Kornev

Research output: Contribution to journalReview articlepeer-review

330 Scopus citations

Abstract

Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to large macromolecular complexes to provide tighter spatiotemporal control. Thus, structural characterization of kinase domains alone is insufficient to explain protein kinase function and regulation in vivo. Recent progress in structural characterization of cyclic AMP-dependent protein kinase (PKA) exemplifies how our knowledge of kinase signalling has evolved by shifting the focus of structural studies from single kinase subunits to macromolecular complexes.

Original languageEnglish
Pages (from-to)646-658
Number of pages13
JournalNature Reviews Molecular Cell Biology
Volume13
Issue number10
DOIs
StatePublished - Oct 2012
Externally publishedYes

Bibliographical note

Funding Information:
Work in the authors’ laboratory is supported by the Howard Hughes Medical Institute and grants from the US National Institutes of Health (NIH) (GM19301, GM34921) and DK54441 to S. S. T.

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