2. Academic Validation
  3. It Takes Two to Tango: Activation of Protein Kinase D by Dimerization

It Takes Two to Tango: Activation of Protein Kinase D by Dimerization

  • Bioessays. 2020 Apr;42(4):e1900222. doi: 10.1002/bies.201900222.
Ronja Reinhardt 1 2,  Linda Truebestein 1 2,  Heiko A Schmidt 3,  Thomas A Leonard 1 2
Affiliations

Affiliations

  • 1 Department of Structural and Computational Biology, Max Perutz Labs, Vienna Biocenter, 1030, Vienna, Austria.
  • 2 Department of Medical Biochemistry, Medical University of Vienna, 1030, Vienna, Austria.
  • 3 Center for Integrative Bioinformatics Vienna, Max Perutz Labs, University of Vienna and Medical University of Vienna, Vienna Biocenter, 1030, Vienna, Austria.
PMID: 31997382 DOI: 10.1002/bies.201900222
Abstract

The recent discovery and structure determination of a novel ubiquitin-like dimerization domain in protein kinase D (PKD) has significant implications for its activation. PKD is a serine/threonine kinase activated by the lipid second messenger diacylglycerol (DAG). It is an essential and highly conserved protein that is implicated in plasma membrane directed trafficking processes from the trans-Golgi network. However, many open questions surround its mechanism of activation, its localization, and its role in the biogenesis of cargo transport carriers. In reviewing this field, the focus is primarily on the mechanisms that control the activation of PKD at precise locations in the cell. In LIGHT of the new structural findings, the understanding of the mechanisms underlying PKD activation is critically evaluated, with particular emphasis on the role of dimerization in PKD autophosphorylation, and the provenance and recognition of the DAG that activates PKD.

Keywords

diacylglycerol; dimerization; lipid; protein kinase D; signaling; structure; ubiquitin-like domain.

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