Α γ-tubulin complex-dependent pathway suppresses ciliogenesis by promoting cilia disassembly

Shankar, Sahana; Hsu, Zi-Ting; Ezquerra, Artur; Li, Chien-Chien; Huang, Tzu-Lun; Coyaud, Étienne; Viais, Ricardo; Grauffel, Cédric; Raught, Brian; Lim, Carmay; Lüders, Jens; Tsai, Su-Yi; Hsia, Kuo‐Chiang

doi:10.1016/j.celrep.2022.111642

Cited by 5 publications

(2 citation statements)

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“…It forms the γ-tubulin ring complex, also known as γ-tuRC, a ring-like structure which serves to nucleate microtubules, both at the centrosome in interphase cells, and at the basal body of the primary cilium when cells exit the cell cycle. In addition, γ-tuRC can modulate cilia disassembly [19, 39]. In MEF wt γ-tubulin showed a clearly defined localization, frequently appearing as two adjacent spots at the base of the cilium, typical of its presence in centrioles [25] (Fig.…”

Section: Resultsmentioning

confidence: 99%

Key role of vimentin in the organization of the primary cilium

Lalioti,

Moneo-Corcuera,

Pérez-Sala

2024

Preprint

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We previously reported the presence of the intermediate filament vimentin at the primary cilium of lung cancer epithelial cells. In this study we further demonstrate that vimentin is intimately intertwined with acetylated tubulin at this structure. Interestingly, although vimentin can be detected along the whole length of the primary cilium, phospho-serine 56 vimentin is found particularly enriched at its basal region in A549 lung cancer cells. Vimentin appears to play a pivotal role in ciliogenesis, since its depletion in MEF or in A549 cells results in a lower proportion of cells displaying primary cilia and recognizable basal bodies. Furthermore, the detectable cilia in vimentin depleted cells are shorter. In addition, the centriolar structure appears disrupted in vimentin deficient cells, as indicated by an abnormal distribution of gamma- and acetylated tubulin. Moreover, these cells display a defective organization of the pericentriolar material, characterized by a marked decrease in the levels of pericentrin and a diffuse distribution of Rab11. Taken together, our results show that vimentin is present at the primary cilium and suggest that it plays an important role in cilium structure and biogenesis, since its depletion leads to marked morphological defects and altered organization of key elements of this structure.

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Section: Resultsmentioning

confidence: 99%

Key role of vimentin in the organization of the primary cilium

Lalioti,

Moneo-Corcuera,

Pérez-Sala

2024

Preprint

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“…Therefore, we examined other cell lines and decided to use SH-SY5Y cells, which express RD3 endogenously 54 and have ciliogenesis capability. 55 , 56 Prior to ciliogenesis analysis, we first examined whether the RD3-mitochondria interaction occurs in SH-SY5Y cells. Using immunocytochemistry analysis, we demonstrated that RD3 co-localized with the mitochondria marker Tomm20 ( Figure 6 A), suggesting that RD3 also interacts with mitochondria in SH-SY5Y cells.…”

Section: Resultsmentioning

confidence: 99%