Format

Send to

Choose Destination
Elife. 2014 Aug 22;3:e03399. doi: 10.7554/eLife.03399.

A molecular mechanism of mitotic centrosome assembly in Drosophila.

Author information

1
Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
2
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
3
Oxford Micron advanced imaging unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Abstract

Centrosomes comprise a pair of centrioles surrounded by pericentriolar material (PCM). The PCM expands dramatically as cells enter mitosis, but it is unclear how this occurs. In this study, we show that the centriole protein Asl initiates the recruitment of DSpd-2 and Cnn to mother centrioles; both proteins then assemble into co-dependent scaffold-like structures that spread outwards from the mother centriole and recruit most, if not all, other PCM components. In the absence of either DSpd-2 or Cnn, mitotic PCM assembly is diminished; in the absence of both proteins, it appears to be abolished. We show that DSpd-2 helps incorporate Cnn into the PCM and that Cnn then helps maintain DSpd-2 within the PCM, creating a positive feedback loop that promotes robust PCM expansion around the mother centriole during mitosis. These observations suggest a surprisingly simple mechanism of mitotic PCM assembly in flies.

KEYWORDS:

D. melanogaster; FRAP; PCM; cell biology; centrosome; centrosome maturation; developmental biology; live super-resolution; stem cells

PMID:
25149451
PMCID:
PMC4175739
DOI:
10.7554/eLife.03399
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for eLife Sciences Publications, Ltd Icon for PubMed Central
Loading ...
Support Center