Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: self- versus non-self-priming.
Mammalian polo-like kinase 1 (Plk1) has been studied intensively as a key element in regulating diverse mitotic events during M-phase progression. Plk1 is spatially regulated through the targeting activity of the conserved polo-box domain (PBD) present in the C-terminal non-catalytic region. Over the years, studies have demonstrated that the PBD forms a phospho-epitope binding module and the PBD-dependent interaction is critical for proper subcellular localization of Plk1. The current prevailing model is that the PBD binds to a phospho-epitope generated by Cdc2 or other Pro-directed kinases. Here we discuss a recent finding that Plk1 also self-promotes its localization by generating its own PBD-docking site.
Lee
Kyung S
KS
Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4258, USA. kyunglee@mail.nih.gov
Park
Jung-Eun
JE
Kang
Young H
YH
Zimmerman
Wendy
W
Soung
Nak-Kyun
NK
Seong
Yeon-Sun
YS
Kwak
Sahng-June
SJ
Erikson
Raymond L
RL
D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008938:Mitosis; D008954:Models, Biological; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000378:metabolism*; D008941:Spindle Apparatus / Q000737:chemistry; D000097869:Polo-Like Kinase 1
D018797:Cell Cycle Proteins; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1