A polo match for Plk1.
New work by Elia et al. in this issue of Cell reveals the molecular basis of phosphopeptide recognition by the polo domain and the domain's dual function to promote substrate recognition by targeting the kinase to subcellular structures and to autoregulate the adjacent protein kinase catalytic domain.
Leung
Genie C
GC
Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada.
Sicheri
Frank
F
D020816:Amino Acid Motifs; D000818:Animals; D001665:Binding Sites; D018797:Cell Cycle Proteins; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D010748:Phosphopeptides / Q000737:chemistry / Q000378:metabolism*; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1
D018797:Cell Cycle Proteins; D005656:Fungal Proteins; D010748:Phosphopeptides; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1