Amorphous no more: subdiffraction view of the pericentriolar material architecture

Mennella, Vito; Agard, David A.; Huang, Bo; Pelletier, Laurence

doi:10.1016/j.tcb.2013.10.001

Cited by 140 publications

(154 citation statements)

References 114 publications

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“…Pioneering work by several labs in 2012 used structured illumination microscopy (SIM) to investigate the spatial distribution of many centrosome proteins (5). These studies showed that pericentrin is an extended molecule with its C terminus (containing the PACT domain) near the centriole wall and its N terminus extending outward.…”

mentioning

confidence: 99%

A centrosomal scaffold shows some self-control

Varadarajan

Hammer

Rusan

2017

Journal of Biological Chemistry

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mentioning

confidence: 99%

A centrosomal scaffold shows some self-control

Varadarajan

Hammer

Rusan

2017

Journal of Biological Chemistry

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“…We notice that the diameter of FIGL-1 ring (about 500 nm) is comparable to that of a typical pericentriolar material (PCM) protein pericentrin. 16,17 Since PCM surrounds mainly around the mother centriole in S and G2 phases when centriole duplication is occurring, 16 FIGL-1 is probably a PCM protein.…”

Section: Overexpressed Figl-1 Damages the Centrosomementioning

confidence: 99%

Fidgetin-like 1 is a ciliogenesis-inhibitory centrosome protein

et al. 2016

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Fidgetin-like 1 (FIGL-1) is a homolog of fidgetin, an AAA protein that was identified as the protein encoded by the gene mutated in fidget mice. Because the phenotypes of fidget mice are reminiscent of the phenotypes of ciliopathy diseases, and because fidgetin has microtubule-severing activity, we hypothesize that these proteins participate in cilia-related processes. Indeed, overexpression of FIGL-1 interfered with ciliogenesis in cultured cells. In particular, overexpressed FIGL-1 strongly accumulated at the centrosome, and, when highly expressed, perturbed the localization of centrosomal proteins such as pericentrin, CP110, and centrin. Using a polyclonal antibody against human FIGL-1, we found that endogenous FIGL-1 localized preferentially around the mother centriole. Consistently, depletion of FIGL-1 by shRNA treatment enhanced ciliogenesis in HEK293T cells. By checking the integrity of the cytoplasmic microtubule network in FIGL-1-overexpressing cells, we found that FIGL-1 probably has microtubule-severing activity, as suggested by its sequence homology with other microtubule-severing proteins. Furthermore, we showed that overexpression of FIGL-1 in zebrafish embryo decreased the length of cilia and perturbed the heart laterality. Taken together, these results demonstrate that FIGL-1 is a new centrosomal protein and inhibits ciliogenesis. These results extend the already long list of centrosomal proteins and provide new insights into the regulation of ciliogenesis.

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“…The proximal ends are believed to be immersed in a cloud of "electron dense" matter [7] [8] [12]- [16]. Therefore, from an electrical perspective, the proximal ends have a negative charge, and the distal ends then have a positive charge.…”

Section: Centriolesmentioning

confidence: 99%

A Review of Centriole Activity, and Wrongful Activity, during Cell Division

Huston¹

2016

ABB

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This is a review paper on centriole behavior and their role in enabling cell division and duplication. The paper is based primarily on articles published in this, the 21 st century. Following a description of centriole geometry, the paper discusses centriole duplication and the ensuring events leading to cell division. From a structural perspective each centriole is seen to be a cylindrical composition of nine blades, each having three microtubules which are themselves hollow cylinders approximately 400 nm long, with inner and outer diameters of 15 and 25 nm. The paper then discusses the nucleation of these microtubules. The paper concludes with a description of centriole malfunction and overduplication (supernumerary centrioles), leading to clusters of centrioles -a hallmark of cancer cells. These centriole clusters thus form "biomarkers" for tumor imaging and treatment.

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Amorphous no more: subdiffraction view of the pericentriolar material architecture

Cited by 140 publications

References 114 publications

A centrosomal scaffold shows some self-control

A centrosomal scaffold shows some self-control

Fidgetin-like 1 is a ciliogenesis-inhibitory centrosome protein

A Review of Centriole Activity, and Wrongful Activity, during Cell Division

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