Cellular and Molecular Life Sciences

, Volume 71, Issue 4, pp 629–639 | Cite as

The cyclin-dependent kinase family in the social amoebozoan Dictyostelium discoideum

  • Robert J. HuberEmail author


Cyclin-dependent kinases (Cdk) are a family of serine/threonine protein kinases that regulate eukaryotic cell cycle progression. Their ability to modulate the cell cycle has made them an attractive target for anti-cancer therapies. Cdk protein function has been studied in a variety of Eukaryotes ranging from yeast to humans. In the social amoebozoan Dictyostelium discoideum, several homologues of mammalian Cdks have been identified and characterized. The life cycle of this model organism is comprised of a feeding stage where single cells grow and divide mitotically as they feed on their bacterial food source and a multicellular developmental stage that is induced by starvation. Thus it is a valuable system for studying a variety of cellular and developmental processes. In this review I summarize the current knowledge of the Cdk protein family in Dictyostelium by highlighting the research efforts focused on the characterization of Cdk1, Cdk5, and Cdk8 in this model Eukaryote. Accumulated evidence indicates that each protein performs distinct functions during the Dictyostelium life cycle with Cdk1 being required for growth and Cdk5 and Cdk8 being required for processes that occur during development. Recent studies have shown that Dictyostelium Cdk5 shares attributes with mammalian Cdk5 and that the mammalian Cdk inhibitor roscovitine can be used to inhibit Cdk5 activity in Dictyostelium. Together, these results show that Dictyostelium can be used as a model system for studying Cdk protein function.


Cyclin-dependent kinase Mitosis Growth Development Cell cycle Dictyostelium 



Adenylyl cyclase A


3′-5′-cyclic adenosine monophosphate




Calmodulin-binding protein


Calmodulin-binding domain


3′-5′-cyclic adenosine monophosphate receptor A


Cyclin-dependent kinase


Cyclin B


Cyclin C


Discoidin 1


Protein kinase A catalytic subunit


Puromycin-sensitive aminopeptidase A



The author would like to thank the anonymous reviewers who provided insightful and helpful feedback during the submission process. This review was supported by a Postdoctoral Fellowship from the Canadian Institutes of Health Research (R.J.H.).


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Copyright information

© Springer Basel 2013

Authors and Affiliations

  1. 1.Center for Human Genetic Research, Massachusetts General Hospital, Harvard Medical SchoolRichard B. Simches Research CenterBostonUSA

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