Involvement of a centrosomal protein kendrin in the maintenance of centrosome cohesion by modulating Nek2A kinase activity

Matsuo, Keitaro; Nishimura, Taiichi; Hayakawa, Akihide; Ono, Yoshitaka; Takahashi, Mikiko

doi:10.1016/j.bbrc.2010.06.063

Cited by 22 publications

(19 citation statements)

References 28 publications

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“…We identified PCNT and Cep215, both products of genes involved in microcephaly syndromes 56, 57 , as interactors of Cep68. PCNT and Cep215 play integral roles in PCM maturation and engagement 22, 31, 33, 36, 58, 59 and interact with each other 32, 54, 60 , sharing a similar localization pattern in mitosis (i.e. increased in prophase and metaphase, and reduced by telophase, when the PCM disassembles and centriole disengagement occurs).…”

Section: Discussionmentioning

confidence: 99%

Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing

Pagan¹,

Marzio²,

Ma³

et al. 2014

Nat Cell Biol

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Summary An intercentrosomal linker keeps the cell’s two centrosomes joined together until it is dissolved at the onset of mitosis. A second connection keeps daughter centrioles engaged to their mothers until they lose their orthogonal arrangement at the end of mitosis. Centriole disengagement is required to license centrioles for duplication. We show that the intercentrosomal linker protein Cep68 is degraded in prometaphase through the SCFβTrCP (Skp1-Cul1-F-box protein) ubiquitin ligase complex. Cep68 degradation is initiated by PLK1 phosphorylation of Cep68 on Ser332, allowing recognition by βTrCP. We also found that Cep68 forms a complex with Cep215/Cdk5Rap2 and PCNT/Pericentrin, two PCM (pericentriolar material) proteins involved in centriole engagement. Cep68 requires two different pools of Cep215. We propose that Cep68 degradation allows Cep215 removal from the peripheral PCM preventing centriole separation following disengagement, whereas PCNT cleavage mediates Cep215 removal from the core of the PCM to inhibit centriole disengagement and duplication.

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Section: Discussionmentioning

confidence: 99%

Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing

Pagan¹,

Marzio²,

Ma³

et al. 2014

Nat Cell Biol

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“…Consistently, siRNA-mediated depletion of pericentrin causes premature centrosome separation in interphase. How pericentrin down-regulates Nek2A kinase activity is unknown; however, the authors proposed a mechanism wherein pericentrin binding changes the overall structure of the protein, flipping the structure of the catalytic domain of Nek2A into an inhibitory conformation (Matsuo et al, 2010). Interestingly, pericentrin and Cep215 localization also depends on Plk1, suggesting an additional level of regulation, either through Nek2A or by direct phosphorylation of some proteins involved in centrosomal cohesion (Graser et al, 2007;Haren et al, 2009).…”

Section: The Function Of Nek2a and Its Upstream Regulationmentioning

confidence: 99%

Breaking the ties that bind: New advances in centrosome biology

Mardin

Schiebel

2012

Journal of Cell Biology

105

132

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The centrosome, which consists of two centrioles and the surrounding pericentriolar material, is the primary microtubule-organizing center (MTOC) in animal cells. Like chromosomes, centrosomes duplicate once per cell cycle and defects that lead to abnormalities in the number of centrosomes result in genomic instability, a hallmark of most cancer cells. Increasing evidence suggests that the separation of the two centrioles (disengagement) is required for centrosome duplication. After centriole disengagement, a proteinaceous linker is established that still connects the two centrioles. In G2, this linker is resolved (centrosome separation), thereby allowing the centrosomes to separate and form the poles of the bipolar spindle. Recent work has identified new players that regulate these two processes and revealed unexpected mechanisms controlling the centrosome cycle.

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“…Pericentrin's function in organizing PCM has been recognized for some time (Doxsey et al ., 1994; Takahashi et al ., 2002; Haren et al ., 2009; Matsuo et al ., 2010). Germane to this function is its ability to properly target and localize to centrosomes, potentially attaching directly to the centriole wall.…”

Section: Introductionmentioning

confidence: 99%

Drosophilapericentrin requires interaction with calmodulin for its function at centrosomes and neuronal basal bodies but not at sperm basal bodies

Galletta

Guillen

Fagerstrom

et al. 2014

MBoC

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Involvement of a centrosomal protein kendrin in the maintenance of centrosome cohesion by modulating Nek2A kinase activity

Cited by 22 publications

References 28 publications

Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing

Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing

Breaking the ties that bind: New advances in centrosome biology

Drosophilapericentrin requires interaction with calmodulin for its function at centrosomes and neuronal basal bodies but not at sperm basal bodies

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