Stogios Peter J, Privé Gilbert G
Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, Canada M5G 2M9.
Trends Biochem Sci. 2004 Dec;29(12):634-7. doi: 10.1016/j.tibs.2004.10.003.
A novel conserved motif--the BACK (for BTB and C-terminal Kelch) domain--is found in the majority of proteins that contain both the BTB domain and kelch repeats. Many kelch-repeat proteins are involved in organization of the cytoskeleton via interaction with actin and intermediate filaments, whereas BTB domains have multiple cellular roles, including recruitment to E3 ubiquitin ligase complexes. The identification of the BACK domain in BTB and kelch proteins, and its high conservation across metazoan genomes, suggest an important function for this domain with a possible role in substrate orientation in Cullin3-based E3 ligase complexes.
在大多数同时包含BTB结构域和kelch重复序列的蛋白质中发现了一种新的保守基序——BACK（BTB和C端Kelch）结构域。许多含kelch重复序列的蛋白质通过与肌动蛋白和中间丝相互作用参与细胞骨架的组织，而BTB结构域具有多种细胞功能，包括募集到E3泛素连接酶复合物。在BTB和kelch蛋白中鉴定出BACK结构域，以及它在多细胞动物基因组中的高度保守性，表明该结构域具有重要功能，可能在基于Cullin3的E3连接酶复合物的底物定向中发挥作用。
