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  Pericentriolar material structure and dynamics.

Woodruff, J., Wueseke, O., & Hyman, A. (2014). Pericentriolar material structure and dynamics. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 369(1650): 20130459.

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 Creators:
Woodruff, Jeffrey1, Author           
Wueseke, Oliver1, Author           
Hyman, Anthony1, Author           
Affiliations:
1Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 Abstract: A centrosome consists of two barrel-shaped centrioles embedded in a matrix of proteins known as the pericentriolar material (PCM). The PCM serves as a platform for protein complexes that regulate organelle trafficking, protein degradation and spindle assembly. Perhaps most important for cell division, the PCM concentrates tubulin and serves as the primary organizing centre for microtubules in metazoan somatic cells. Thus, similar to other well-described organelles, such as the nucleus and mitochondria, the cell has compartmentalized a multitude of vital biochemical reactions in the PCM. However, unlike these other organelles, the PCM is not membrane bound, but rather a dynamic collection of protein complexes and nucleic acids that constitute the organelle's interior and determine its boundary. How is the complex biochemical machinery necessary for the myriad centrosome functions concentrated and maintained in the PCM? Recent advances in proteomics and RNAi screening have unveiled most of the key PCM components and hinted at their molecular interactions ( table 1). Now we must understand how the interactions between these molecules contribute to the mesoscale organization and the assembly of the centrosome. Among outstanding questions are the intrinsic mechanisms that determine PCM shape and size, and how it functions as a biochemical reaction hub.

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 Dates: 2014
 Publication Status: Issued
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 Identifiers: eDoc: 705692
Other: 5847
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Title: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
Source Genre: Journal
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Pages: - Volume / Issue: 369 (1650) Sequence Number: 20130459 Start / End Page: - Identifier: -