Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68

Ella Czarina Morishita, Kazutaka Murayama, Miyuki Kato-Murayama, Yoshiko Ishizuka-Katsura, Yuri Tomabechi, Tomoatsu Hayashi, Takaho Terada, Noriko Handa, Mikako Shirouzu, Tetsu Akiyama, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Adenomatous polyposis coli (APC) is a tumor suppressor protein commonly mutated in colorectal tumors. APC plays important roles in Wnt signaling and other cellular processes. Here, we present the crystal structure of the armadillo repeat (Arm) domain of APC, which facilitates the binding of APC to various proteins. APC-Arm forms a superhelix with a positively charged groove. We also determined the structure of the complex of APC-Arm with the tyrosine-rich (YY) domain of the Src-associated in mitosis, 68 kDa protein (Sam68), which regulates TCF-1 alternative splicing. Sam68-YY forms numerous interactions with the residues on the groove and is thereby fixed in a bent conformation. We assessed the effects of mutations and phosphorylation on complex formation between APC-Arm and Sam68-YY. Structural comparisons revealed different modes of ligand recognition between the Arm domains of APC and other Arm-containing proteins.

Original languageEnglish
Pages (from-to)1496-1508
Number of pages13
JournalStructure
Volume19
Issue number10
DOIs
Publication statusPublished - 2011 Oct 12

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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