Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-49583
J Cell Biol November 24, 2014; 207 (4): 499-516.
Show Gene links Show Anatomy links

Dynein light intermediate chains maintain spindle bipolarity by functioning in centriole cohesion.

Jones LA , Villemant C , Starborg T , Salter A , Goddard G , Ruane P , Woodman PG , Papalopulu N , Woolner S , Allan VJ .


Abstract
Cytoplasmic dynein 1 (dynein) is a minus end-directed microtubule motor protein with many cellular functions, including during cell division. The role of the light intermediate chains (LICs; DYNC1LI1 and 2) within the complex is poorly understood. In this paper, we have used small interfering RNAs or morpholino oligonucleotides to deplete the LICs in human cell lines and Xenopus laevis early embryos to dissect the LICs'' role in cell division. We show that although dynein lacking LICs drives microtubule gliding at normal rates, the LICs are required for the formation and maintenance of a bipolar spindle. Multipolar spindles with poles that contain single centrioles were formed in cells lacking LICs, indicating that they are needed for maintaining centrosome integrity. The formation of multipolar spindles via centrosome splitting after LIC depletion could be rescued by inhibiting Eg5. This suggests a novel role for the dynein complex, counteracted by Eg5, in the maintenance of centriole cohesion during mitosis.

PubMed ID: 25422374
PMC ID: PMC4242835
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: cenpe cetn3 ctrl dnai1 dync1li1 gnl3 h2bc21 kif11 lmna nuf2 tub
Morpholinos: dync1li1 MO1 dync1li2 MO1


Article Images: [+] show captions
References [+] :
Addinall, Phosphorylation by cdc2-CyclinB1 kinase releases cytoplasmic dynein from membranes. 2001, Pubmed, Xenbase