Abstract:
:Cytokinesis in metazoan cells requires a set of antiparallel microtubules that become bundled upon anaphase onset to form a structure known as the central spindle. Bundling of these microtubules requires a protein complex, centralspindlin, that consists of the CYK-4/MgcRacGAP Rho-family GTPase-activating protein and the ZEN-4/MKLP1 kinesin-6 motor protein. Centralspindlin, but not its individual subunits, is sufficient to bundle microtubules in vitro. Here, we present a biochemical and genetic dissection of centralspindlin. We show that each of the two subunits of centralspindlin dimerize via a parallel coiled coil. The two homodimers assemble into a high-affinity heterotetrameric complex by virtue of two low-affinity interactions. Conditional mutations in the regions that mediate complex assembly can be readily suppressed by numerous second site mutations in the interacting regions. This unexpected plasticity explains the lack of primary sequence conservation of the regions critical for this essential protein-protein interaction.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Pavicic-Kaltenbrunner V,Mishima M,Glotzer Mdoi
10.1091/mbc.e07-05-0468subject
Has Abstractpub_date
2007-12-01 00:00:00pages
4992-5003issue
12eissn
1059-1524issn
1939-4586pii
E07-05-0468journal_volume
18pub_type
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