2LL2

Structure of the Cx43 C-terminal domain bound to tubulin

2LL2 の概要

• エントリーDOI: 10.2210/pdb2ll2/pdb
• NMR情報: BMRB: 18022
• 分子名称: Gap junction alpha-1 protein (1 entity in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P17302
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2720.07

構造登録者

Saidi Brikci-Nigassa, A.,Clement, M.,Ha-Duong, T.,Benmansour, K.,Adjadj, E.,Ziani, L.,Pastre, D.,Curmi, P.A. (登録日: 2011-10-26, 公開日: 2012-06-20, 最終更新日: 2024-05-15)

主引用文献

Saidi Brikci-Nigassa, A.,Clement, M.J.,Ha-Duong, T.,Adjadj, E.,Ziani, L.,Pastre, D.,Curmi, P.A.,Savarin, P.
Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules.
Biochemistry, 51:4331-4342, 2012

PubMed Abstract: Connexins are structurally related transmembrane proteins that assemble to form gap junction channels involved in the mediation of intercellular communication. It has been shown that the intracellular tail of connexin43 (Cx43) interacts with tubulin and microtubules with putative impacts on its own intracellular trafficking, its activity in channel communication, and its interference with specific growth factor signal transduction cascades. We demonstrate here that the microtubule binding of Cx43 is mainly driven by a short region of 26 amino acid residues located within the intracellular tail of Cx43. The nuclear magnetic resonance structural analysis of a peptide (K26D) corresponding to this region shows that this peptide is unstructured when free in solution and adopts a helix conformation upon binding with tubulin. In addition, the resulting K26D-tubulin molecular complex defines a new structural organization that could be shared by other microtubule partners. Interestingly, the K26D-tubulin interaction is prevented by the phosphorylation of K26D at a src kinase specific site. Altogether, the results elucidate the mechanism of the interaction of Cx43 with the microtubule cytoskeleton and propose a pathway for understanding the microtubule-dependent regulation of Cx43 gap junctional communications and the involvement of Cx43 in TGF-β signal transduction.

PubMed: 22558917
DOI: 10.1021/bi201806j

実験手法

SOLUTION NMR