2010
DOI: 10.1242/jcs.068502
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Plk4 trans-autophosphorylation regulates centriole number by controlling βTrCP-mediated degradation

Abstract: Centrioles are the main constituents of the mammalian centrosome and act as basal bodies for ciliogenesis. Centrosomes organize the cytoplasmic microtubule network during interphase and the mitotic spindle during mitosis, and aberrations in centrosome number have been implicated in chromosomal instability and tumor formation. The centriolar protein Polo-like kinase 4 (Plk4) is a key regulator of centriole biogenesis and is crucial for maintaining constant centriole number, but the mechanisms regulating its act… Show more

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Cited by 199 publications
(300 citation statements)
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“…Our measurements now allow us to put a specific number to this term. Levels of Plk4 are remarkably similar in all cells analyzed, in line with the notion that human Plk4 is subject to tight autoregulation through proteolytic degradation (Guderian et al , 2010; Holland et al , 2010). STIL is expressed at similarly low levels as Plk4, but expression of Sas‐6 shows surprisingly high variation between cell lines.…”
Section: Discussionsupporting
confidence: 81%
See 1 more Smart Citation
“…Our measurements now allow us to put a specific number to this term. Levels of Plk4 are remarkably similar in all cells analyzed, in line with the notion that human Plk4 is subject to tight autoregulation through proteolytic degradation (Guderian et al , 2010; Holland et al , 2010). STIL is expressed at similarly low levels as Plk4, but expression of Sas‐6 shows surprisingly high variation between cell lines.…”
Section: Discussionsupporting
confidence: 81%
“…Centriole formation is initiated by the protein kinase Plk4 (also known as Sak; Bettencourt‐Dias et al , 2005; Habedanck et al , 2005), which undergoes activation through trans‐autophosphorylation at a T‐loop residue (Lopes et al , 2015). Steady‐state cellular levels of Plk4 are generally kept low through trans‐autophosphorylation of a DSG‐motif and subsequent degradation by SCF‐β‐TrCP (Guderian et al , 2010; Holland et al , 2010). Plk4 assembles at the surface of mother centrioles through binding to Cep152 and Cep192 (Cizmecioglu et al , 2010; Hatch et al , 2010; Kim et al , 2013; Sonnen et al , 2013; Park et al , 2014).…”
Section: Introductionmentioning
confidence: 99%
“…If this system fails, the consequence is development of multiple centrioles both in Drosophila and human cells. Plk4 degradation first requires that Plk4 forms a homodimer through its carboxy-terminal coiledcoil region (Leung et al 2002;Habedanck et al 2005), where it is able to autophosphorylate a phosphodegron enabling the binding of SCF Slimb/bTrCP to promote its own destruction (Guderian et al 2010;Holland et al 2010Holland et al , 2012Sillibourne et al 2010). Consistently, the ZYG-1 kinase of C. elegans is also down-regulated by the Slimb/bTrCP homolog, LIN-23, and also a second F-box protein, SEL-10 (Peel et al 2012).…”
Section: Plk4mentioning
confidence: 97%
“…In contrast, we know quite a lot about the controlled proteolysis of Plk4 kinase that is achieved in both Drosophila and human cells via the SCF Slimb/bTrCP ubiquitin ligase complex (Cunha-Ferreira et al 2009;Rogers et al 2009;Guderian et al 2010). If this system fails, the consequence is development of multiple centrioles both in Drosophila and human cells.…”
Section: Plk4mentioning
confidence: 99%
“…It is therefore possible that the overexpressed p.(M148V) variant does not reduce the overall kinase activity levels of PLK4 in the presence of the WT protein even if it lacks kinase activity itself. 18 Western blot analysis of overexpressed PLK4 suggests that the p.(M148V) variant has slightly less activity than WT. Although the exact function of the M148 residue has not yet been characterized, the strong evolutionary conservation of this residue suggests that it has functional importance.…”
Section: Discussionmentioning
confidence: 98%