scholarly journals Drosophila Ana2 is a conserved centriole duplication factor

2010 ◽  
Vol 188 (3) ◽  
pp. 313-323 ◽  
Author(s):  
Naomi R. Stevens ◽  
Jeroen Dobbelaere ◽  
Kathrin Brunk ◽  
Anna Franz ◽  
Jordan W. Raff

In Caenorhabditis elegans, five proteins are required for centriole duplication: SPD-2, ZYG-1, SAS-5, SAS-6, and SAS-4. Functional orthologues of all but SAS-5 have been found in other species. In Drosophila melanogaster and humans, Sak/Plk4, DSas-6/hSas-6, and DSas-4/CPAP—orthologues of ZYG-1, SAS-6, and SAS-4, respectively—are required for centriole duplication. Strikingly, all three fly proteins can induce the de novo formation of centriole-like structures when overexpressed in unfertilized eggs. Here, we find that of eight candidate duplication factors identified in cultured fly cells, only two, Ana2 and Asterless (Asl), share this ability. Asl is now known to be essential for centriole duplication in flies, but no equivalent protein has been found in worms. We show that Ana2 is the likely functional orthologue of SAS-5 and that it is also related to the vertebrate STIL/SIL protein family that has been linked to microcephaly in humans. We propose that members of the SAS-5/Ana2/STIL family of proteins are key conserved components of the centriole duplication machinery.

Gene ◽  
2001 ◽  
Vol 263 (1-2) ◽  
pp. 219-230 ◽  
Author(s):  
Ian G Frame ◽  
John F Cutfield ◽  
Russell T.M Poulter

Author(s):  
Raquel Borges de Barros Primo ◽  
Jacenir Vieira da Silva ◽  
Larissa P. Mueller ◽  
Flávio H. S. Araújo ◽  
Silvia Aparecida Oesterreich

Author(s):  
Margarita Elena Papandreou ◽  
Konstantinos Palikaras ◽  
Nektarios Tavernarakis

2019 ◽  
Vol 14 (5) ◽  
pp. 1455-1488 ◽  
Author(s):  
Matthew A. Churgin ◽  
Milan Szuperak ◽  
Kristen C. Davis ◽  
David M. Raizen ◽  
Christopher Fang-Yen ◽  
...  

2015 ◽  
Vol 211 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Vineet Choudhary ◽  
Namrata Ojha ◽  
Andy Golden ◽  
William A. Prinz

Lipid droplets (LDs) are found in all cells and play critical roles in lipid metabolism. De novo LD biogenesis occurs in the endoplasmic reticulum (ER) but is not well understood. We imaged early stages of LD biogenesis using electron microscopy and found that nascent LDs form lens-like structures that are in the ER membrane, raising the question of how these nascent LDs bud from the ER as they grow. We found that a conserved family of proteins, fat storage-inducing transmembrane (FIT) proteins, is required for proper budding of LDs from the ER. Elimination or reduction of FIT proteins in yeast and higher eukaryotes causes LDs to remain in the ER membrane. Deletion of the single FIT protein in Caenorhabditis elegans is lethal, suggesting that LD budding is an essential process in this organism. Our findings indicated that FIT proteins are necessary to promote budding of nascent LDs from the ER.


1992 ◽  
Vol 89 (9) ◽  
pp. 4168-4172 ◽  
Author(s):  
S. P. Rohrer ◽  
P. T. Meinke ◽  
E. C. Hayes ◽  
H. Mrozik ◽  
J. M. Schaeffer

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