PDBsum entry 2lyc

Protein binding

PDB id: 2lyc

Contents

Protein chain

130 a.a.

PDB id:

2lyc

Name:

Protein binding

Title:

Structure of c-terminal domain of ska1

Structure:

Spindle and kinetochore-associated protein 1 homolog. Chain: a. Fragment: c-terminal domain. Engineered: yes

Source:

Caenorhabditis elegans. Nematode. Organism_taxid: 6239. Gene: y106g6h.15. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

A.Boeszoermenyi,J.C.Schmidt,M.Markus,M.Oberer,I.M.Cheeseman,G.Wagner, H.Arthanari

Key ref:

J.C.Schmidt et al. (2012). The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and binds to curved protofilaments. Dev Cell, 23, 968-980. PubMed id: 23085020

Date:

14-Sep-12 Release date: 24-Oct-12

Protein chain

Q9XWS0  (SKA1_CAEEL) -  Spindle and kinetochore-associated protein 1 from Caenorhabditis elegans

Seq: 243 a.a.

Struc: 130 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

Dev Cell 23:968-980 (2012)

PubMed id: 23085020

The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and binds to curved protofilaments.

J.C.Schmidt, H.Arthanari, A.Boeszoermenyi, N.M.Dashkevich, E.M.Wilson-Kubalek, N.Monnier, M.Markus, M.Oberer, R.A.Milligan, M.Bathe, G.Wagner, E.L.Grishchuk, I.M.Cheeseman.

ABSTRACT

To ensure equal chromosome segregation during mitosis, the macromolecular kinetochore must remain attached to depolymerizing microtubules, which drive chromosome movements. How kinetochores associate with depolymerizing microtubules, which undergo dramatic structural changes forming curved protofilaments, has yet to be defined in vertebrates. Here, we demonstrate that the conserved kinetochore-localized Ska1 complex tracks with depolymerizing microtubule ends and associates with both the microtubule lattice and curved protofilaments. In contrast, the Ndc80 complex, a central player in the kinetochore-microtubule interface, binds only to the straight microtubule lattice and lacks tracking activity. We demonstrate that the Ska1 complex imparts its tracking capability to the Ndc80 complex. Finally, we present a structure of the Ska1 microtubule-binding domain that reveals its interaction with microtubules and its regulation by Aurora B. This work defines an integrated kinetochore-microtubule interface formed by the Ska1 and Ndc80 complexes that associates with depolymerizing microtubules, potentially by interacting with curved microtubule protofilaments.