Trichoplein and Aurora A block aberrant primary cilia assembly in proliferating cells

Inoko, Akihito; Matsuyama, Makoto; Goto, Hidemasa; Ohmuro‐Matsuyama, Yuki; Hayashi, Yuko; Enomoto, Mika; Ibi, Miho; Urano, Takeshi; Yonemura, Shigenobu; Kiyono, Tohru; Izawa, Ichiro; Inagaki, Masaki

doi:10.1083/jcb.201106101

Cited by 133 publications

(255 citation statements)

References 52 publications

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“…1A and B). Several recent studies demonstrate that the presence of primary cilia can delay the cell cycle, 9,[25][26][27][28] suggesting that the presence of primary cilia in VDAC3-and Mps1-depleted cells may account for the cell cycle delay. Thus, we set out to determine whether VDAC3 and Mps1 might regulate ciliogenesis.…”

Section: Resultsmentioning

confidence: 99%

“…7 Recent studies indicate that various molecular machineries that control the temporal switch between basal bodies and centrioles play a crucial role in regulating ciliary assembly-disassembly in co-ordination with the cell cycle. [8][9][10][11][12] Defects in the assembly or function of primary cilia are associated with a series of pathologies broadly known as ciliopathies. 13,14 We have recently shown voltage-dependent anion channel 3 (VDAC3), a mitochondrial porin, to localize to centrosomes, preferentially to the mother centriole and to interact with the centrosomal protein kinase Mps1, which was also predominantly associated with the mother centriole.…”

Section: Introductionmentioning

confidence: 99%

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VDAC3 and Mps1 negatively regulate ciliogenesis

Majumder

Fisk

2013

Cell Cycle

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

VDAC3 and Mps1 negatively regulate ciliogenesis

Majumder

Fisk

2013

Cell Cycle

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“…AURKA has been implicated in deciliation in Chlamydomonas (Pan et al, 2004) and retinal pigment epithelial (RPE)1 cells, where AURKA has been shown to be activated by HEF1 to promote activation of HDAC6, causing deacetylation and destabilization of axonemal microtubules (Pugacheva et al, 2007), although the importance of HDAC6 for deciliation has been questioned (Goto et al, 2013). Subsequent reports have confirmed the role of AURKA in deciliation and identified additional factors that regulate its activity, including calmodulin (CaM) (Plotnikova et al, 2012), PLK1 (Lee et al, 2012), Pitchfork (Kinzel et al, 2010), Trichoplein (Inoko et al, 2012) and Peroxiredoxin 1 (Gong et al, 2014).…”

Section: Introductionmentioning

confidence: 90%

PDGFRβ and oncogenic, mutant PDGFRα D842V promote disassembly of primary cilia by a PLCγ and AURKA dependent mechanism

Nielsen

Malinda

Schmid

et al. 2015

Journal of Cell Science

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Primary cilia are microtubule-based sensory organelles projecting from most quiescent mammalian cells, which disassemble in cells cultured in serum-deprived conditions upon re-addition of serum or growth factors. Platelet-derived growth factors (PDGF) are implicated in deciliation, but the specific receptor isoforms and mechanisms involved are unclear. We report that PDGFRβ promotes deciliation in cultured cells and provide evidence implicating PLCγ and intracellular Ca 2+ release in this process. Activation of wild-type PDGFRα alone did not elicit deciliation. However, expression of constitutively active PDGFRα D842V mutant receptor, which potently activates PLCγ (also known as PLCG1), caused significant deciliation, and this phenotype was rescued by inhibiting PDGFRα D842V kinase activity or AURKA. We propose that PDGFRβ and PDGFRα D842V promote deciliation through PLCγ-mediated Ca 2+ release from intracellular stores, causing activation of calmodulin and AURKA-triggered deciliation.

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“…Transmission electron microscopy was performed in essentially the same manner as described elsewhere 38 . In brief, HeLa-K cells cultured on coverslips were fixed with 2% fresh formaldehyde and 2.5% glutaraldehyde in 0.1 M sodium cacodylate buffer, pH 7.4, for 2 h at RT.…”

Section: Methodsmentioning

confidence: 99%

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

et al. 2014

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Recent studies have revealed the presence of a microtubule subpopulation called Golgi-derived microtubules that support Golgi ribbon formation, which is required for maintaining polarized cell migration. CLASPs and AKAP450/CG-NAP are involved in their formation, but the underlying molecular mechanisms remain unclear. Here, we find that the microtubule-crosslinking protein, MTCL1, is recruited to the Golgi membranes through interactions with CLASPs and AKAP450/CG-NAP, and promotes microtubule growth from the Golgi membrane. Correspondingly, MTCL1 knockdown specifically impairs the formation of the stable perinuclear microtubule network to which the Golgi ribbon tethers and extends. Rescue experiments demonstrate that besides its crosslinking activity mediated by the N-terminal microtubule-binding region, the C-terminal microtubule-binding region plays essential roles in these MTCL1 functions through a novel microtubule-stabilizing activity. These results suggest that MTCL1 cooperates with CLASPs and AKAP450/CG-NAP in the formation of the Golgi-derived microtubules, and mediates their development into a stable microtubule network.

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Trichoplein and Aurora A block aberrant primary cilia assembly in proliferating cells

Abstract: The trichoplein–AurA pathway must suppress primary cilia assembly in order for cells to exit G1.

Cited by 133 publications

References 52 publications

VDAC3 and Mps1 negatively regulate ciliogenesis

VDAC3 and Mps1 negatively regulate ciliogenesis

PDGFRβ and oncogenic, mutant PDGFRα D842V promote disassembly of primary cilia by a PLCγ and AURKA dependent mechanism

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

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