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Amorphous no more: subdiffraction view of the pericentriolar material architecture

Amorphous no more: subdiffraction view of the pericentriolar material architecture
Amorphous no more: subdiffraction view of the pericentriolar material architecture

The centrosome influences the shape, orientation and activity of the microtubule cytoskeleton. The pericentriolar material (PCM), determines this functionality by providing a dynamic platform for nucleating microtubules and acts as a nexus for molecular signaling. Although great strides have been made in understanding PCM activity, its diffraction-limited size and amorphous appearance on electron microscopy (EM) have limited analysis of its high-order organization. Here, we outline current knowledge of PCM architecture and assembly, emphasizing recent super-resolution imaging studies that revealed the PCM has a layered structure made of fibers and matrices conserved from flies to humans. Notably, these studies debunk the long-standing view of an amorphous PCM and provide a paradigm to dissect the supramolecular organization of organelles in cells.

Centrioles/ultrastructure, Centrosome/ultrastructure, Humans, Microscopy, Electron, Microtubules/ultrastructure
0962-8924
188-197
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Agard, David A
c0733eec-3b98-4a05-9cac-4a965769f5b1
Huang, Bo
d14fc43d-520a-4944-9897-13303670751c
Pelletier, Laurence
51e7e63d-8c62-4459-b8cd-6aeddc4a3692
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Agard, David A
c0733eec-3b98-4a05-9cac-4a965769f5b1
Huang, Bo
d14fc43d-520a-4944-9897-13303670751c
Pelletier, Laurence
51e7e63d-8c62-4459-b8cd-6aeddc4a3692

Mennella, Vito, Agard, David A, Huang, Bo and Pelletier, Laurence (2014) Amorphous no more: subdiffraction view of the pericentriolar material architecture. Trends in Cell Biology, 24 (3), 188-197. (doi:10.1016/j.tcb.2013.10.001).

Record type: Review

Abstract

The centrosome influences the shape, orientation and activity of the microtubule cytoskeleton. The pericentriolar material (PCM), determines this functionality by providing a dynamic platform for nucleating microtubules and acts as a nexus for molecular signaling. Although great strides have been made in understanding PCM activity, its diffraction-limited size and amorphous appearance on electron microscopy (EM) have limited analysis of its high-order organization. Here, we outline current knowledge of PCM architecture and assembly, emphasizing recent super-resolution imaging studies that revealed the PCM has a layered structure made of fibers and matrices conserved from flies to humans. Notably, these studies debunk the long-standing view of an amorphous PCM and provide a paradigm to dissect the supramolecular organization of organelles in cells.

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More information

e-pub ahead of print date: 19 November 2013
Published date: March 2014
Keywords: Centrioles/ultrastructure, Centrosome/ultrastructure, Humans, Microscopy, Electron, Microtubules/ultrastructure

Identifiers

Local EPrints ID: 434095
URI: http://eprints.soton.ac.uk/id/eprint/434095
ISSN: 0962-8924
PURE UUID: afbf15c0-878c-441a-8a0b-42ef93020087
ORCID for Vito Mennella: ORCID iD orcid.org/0000-0002-4842-9012

Catalogue record

Date deposited: 12 Sep 2019 16:30
Last modified: 16 Mar 2024 04:04

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Contributors

Author: Vito Mennella ORCID iD
Author: David A Agard
Author: Bo Huang
Author: Laurence Pelletier

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