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  The Caenorhabditis elegans pericentriolar material components SPD-2 and SPD-5 are monomeric in the cytoplasm before incorporation into the PCM matrix

Wueseke, O., Bunkenborg, J., Hein, M. Y., Zinke, A., Viscardi, V., Woodruff, J. B., et al. (2014). The Caenorhabditis elegans pericentriolar material components SPD-2 and SPD-5 are monomeric in the cytoplasm before incorporation into the PCM matrix. MOLECULAR BIOLOGY OF THE CELL, 25(19), 2984-2992. doi:10.1091/mbc.E13-09-0514.

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 Creators:
Wueseke, Oliver1, Author
Bunkenborg, Jakob1, Author
Hein, Marco Y.2, Author           
Zinke, Andrea1, Author
Viscardi, Valeria1, Author
Woodruff, Jeffrey B.1, Author
Oegema, Karen1, Author
Mann, Matthias2, Author           
Andersen, Jens S.1, Author
Hyman, Anthony A.1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: CROSS-CORRELATION SPECTROSCOPY; FLUORESCENCE CORRELATION SPECTROSCOPY; C-ELEGANS; CENTROSOME DUPLICATION; PROTEIN INTERACTIONS; EARLY EMBRYOGENESIS; LIVING CELLS; IN-VIVO; MATURATION; CENTRIOLAR
 Abstract: Centrosomes are the main microtubule-organizing centers in animal cells. Centrosomes consist of a pair of centrioles surrounded by a matrix of pericentriolar material (PCM) that assembles from cytoplasmic components. In Caenorhabditis elegans embryos, interactions between the coiled-coil proteins SPD-5 and SPD-2 and the kinase PLK-1 are critical for PCM assembly. However, it is not known whether these interactions promote the formation of cytoplasmic complexes that are added to the PCM or whether the components interact only during incorporation into the PCM matrix. Here we address this problem by using a combination of live-cell fluorescence correlation spectroscopy, mass spectrometry, and hydrodynamic techniques to investigate the native state of PCM components in the cytoplasm. We show that SPD-2 is monomeric, and neither SPD-2 nor SPD-5 exists in complex with PLK-1. SPD-5 exists mostly as a monomer but also forms complexes with the PP2A-regulatory proteins RSA-1 and RSA-2, which are required for microtubule organization at centrosomes. These results suggest that the interactions between SPD-2, SPD-5, and PLK-1 do not result in formation of cytoplasmic complexes, but instead occur in the context of PCM assembly.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000343124100009
DOI: 10.1091/mbc.E13-09-0514
 Degree: -

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Title: MOLECULAR BIOLOGY OF THE CELL
Source Genre: Journal
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Publ. Info: 8120 WOODMONT AVE, STE 750, BETHESDA, MD 20814-2755 USA : AMER SOC CELL BIOLOGY
Pages: - Volume / Issue: 25 (19) Sequence Number: - Start / End Page: 2984 - 2992 Identifier: ISSN: 1059-1524