A role for Gle1, a regulator of DEAD-box RNA helicases, at centrosomes and basal bodies

• Published in: Molecular biology of the cell 2017-01, Vol.28 (1), p.120-127
• Main Authors: Jao, Li-En, Akef, Abdalla, Wente, Susan R
• Format: Article
• Language: English
• Subjects: Active Transport, Cell Nucleus; Adenosine Triphosphatases; Antigens - metabolism; Basal Bodies - metabolism; Centrosome - metabolism; DEAD-box RNA Helicases - metabolism; Nuclear Pore - metabolism; Nuclear Pore Complex Proteins - metabolism; Nucleocytoplasmic Transport Proteins - metabolism; Protein Binding; RNA Transport; RNA, Messenger - metabolism; RNA-Binding Proteins - metabolism; RNA-Binding Proteins - physiology; Zebrafish Proteins - metabolism; Zebrafish Proteins - physiology
• ISSN: 1059-1524; 1939-4586
• DOI: 10.1091/mbc.e16-09-0675

Control of organellar assembly and function is critical to eukaryotic homeostasis and survival. Gle1 is a highly conserved regulator of RNA-dependent DEAD-box ATPase proteins, with critical roles in both mRNA export and translation. In addition to its well-defined interaction with nuclear pore complexes, here we find that Gle1 is enriched at the centrosome and basal body. Gle1 assembles into the toroid-shaped pericentriolar material around the mother centriole. Reduced Gle1 levels are correlated with decreased pericentrin localization at the centrosome and microtubule organization defects. Of importance, these alterations in centrosome integrity do not result from loss of mRNA export. Examination of the Kupffer's vesicle in Gle1-depleted zebrafish revealed compromised ciliary beating and developmental defects. We propose that Gle1 assembly into the pericentriolar material positions the DEAD-box protein regulator to function in localized mRNA metabolism required for proper centrosome function.