A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies
A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of Plk4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of Plk4 and the coiled-coil dom...
Main Authors: | Cottee, M, Johnson, S, Raff, J, Lea, S |
---|---|
Format: | Journal article |
Language: | English |
Published: |
Company of Biologists
2017
|
Similar Items
-
Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
by: Liu, Y, et al.
Published: (2018) -
Crystal structures of the CPAP/STIL complex reveal its role in centriole assembly and human microcephaly
by: Cottee, M, et al.
Published: (2013) -
SAS-6 oligomerization: the key to the centriole?
by: Cottee, M, et al.
Published: (2011) -
The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies.
by: Cottee, M, et al.
Published: (2015) -
Centrioles generate a local pulse of Polo/PLK1 activity to initiate mitotic centrosome assembly
by: Wong, S-S, et al.
Published: (2022)