 |
PDBsum entry 3vza
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Cenp-T provides a structural platform for outer kinetochore assembly.
|
|
|
Authors
|
|
T.Nishino,
F.Rago,
T.Hori,
K.Tomii,
I.M.Cheeseman,
T.Fukagawa.
|
|
|
Ref.
|
|
Embo J, 2013,
32,
424-436.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The kinetochore forms a dynamic interface with microtubules from the mitotic
spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding
complex at kinetochores. However, it is unclear how the Ndc80 complex associates
with the inner kinetochore proteins that assemble upon centromeric chromatin.
Here, based on a high-resolution structural analysis, we demonstrate that the
N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the
Spc24/25 portion of the Ndc80 complex. Phosphorylation of CENP-T strengthens a
cryptic hydrophobic interaction between CENP-T and Spc25 resulting in a
phospho-regulated interaction that occurs without direct recognition of the
phosphorylated residue. The Ndc80 complex interacts with both CENP-T and the
Mis12 complex, but we find that these interactions are mutually exclusive,
supporting a model in which two distinct pathways target the Ndc80 complex to
kinetochores. Our results provide a model for how the multiple protein complexes
at kinetochores associate in a phospho-regulated manner.
|
|
|
|
|
|
|
