The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKγ

Kohei Saito, Takanori Kigawa, Seizo Koshiba, Kazuo Sato, Yo Matsuo, Ayako Sakamoto, Tetsuo Takagi, Mikako Shirouzu, Takashi Yabuki, Emi Nunokawa, Eiko Seki, Takayoshi Matsuda, Masaaki Aoki, Yukako Miyata, Noriko Hirakawa, Makoto Inoue, Takaho Terada, Takahiro Nagase, Reiko Kikuno, Manabu NakayamaOsamu Ohara, Akiko Tanaka, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

80 Citations (Scopus)

Abstract

CYLD was originally identified as the human familial cylindromatosis tumor suppressor. Recently, it was reported that CYLD directly interacts with NEMO/IKKγ and TRAF2 in the NF-κB signaling pathway. The two proteins bind to a region of CYLD that contains a Cys-box motif and the third cytoskeleton-associated protein-glycine conserved (CAP-Gly) domain. Here we report that the third CAP-Gly domain of CYLD specifically interacts with one of the two proline-rich sequences of NEMO/IKKγ. The tertiary structure of the CAP-Gly domain shares the five-stranded β sheet topology with the SH3 domain, which is well known as a proline-rich sequence-recognition domain. However, chemical shift mapping revealed that the peptide binding site of the CAP-Gly domain is formed without the long peptide binding loop characteristic of the SH3 domain. Therefore, CAP-Gly is likely to be a novel proline-rich sequence binding domain with a mechanism different from that of the SH3 domain.

Original languageEnglish
Pages (from-to)1719-1728
Number of pages10
JournalStructure
Volume12
Issue number9
DOIs
Publication statusPublished - 2004 Sep
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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