title: Perspectives in PDK1 evolution: insights from photosynthetic and non-photosynthetic organisms.
abstract: Protein kinases belonging to the AGC group modulate many diverse cellular processes in all eukaryotes. One important way to regulate AGC kinases is through phosphorylation by the upstream kinase PDK1. PDK1 localization and activity usually depend on interactions with phospholipids, which are mediated by a conserved lipid-binding pleckstrin homology (PH) domain. We recently analyzed putative PDK1 sequences from 17 photosynthetic organisms, finding that PDK1s from vascular and nonvascular species seem to be distinguished by the presence or absence of a PH domain, respectively. The only other reported PDK1 lacking a PH domain is from yeast (Saccharomyces cerevisiae). These observations raise questions about how plant PDK1s and their lipid-binding capabilities have evolved in relation to other eukaryotes, and what this means for PDK1 function. Here we use 100 PDK1 sequences from diverse organisms to discuss possible evolutionary aspects of plant PDK1 structure and lipid binding.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
authors.forename: Anna C Nelson
authors.initials: AC
authors.lastname: Dittrich
authors.forename: Timothy P
authors.initials: TP
authors.lastname: Devarenne
mesh_terms: D064413:3-Phosphoinositide-Dependent Protein Kinases; D019143:Evolution, Molecular; D050356:Lipid Metabolism; D010788:Photosynthesis; D010802:Phylogeny; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics*
chemical_list: D064413:3-Phosphoinositide-Dependent Protein Kinases; D017346:Protein Serine-Threonine Kinases