Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules

Byeong Gu Han, Kyoung Hoon Kim, Sang Jae Lee, Kyung Chae Jeong, Jea Won Cho, Kyung Hee Noh, Tae Woo Kim, Soon Jong Kim, Hye Jin Yoon, Se Won Suh, Sangho Lee, Byung Il Lee

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Apoptosis inhibitor 5 (API5) is an anti-apoptotic protein that is up-regulated in various cancer cells. Here, we present the crystal structure of human API5. API5 exhibits an elongated all α-helical structure. The N-terminal half of API5 is similar to the HEAT repeat and the C-terminal half is similar to the ARM (Armadillo-like) repeat. HEAT and ARM repeats have been implicated in protein-protein interactions, suggesting that the cellular roles of API5 may be to mediate protein-protein interactions. Various components of multiprotein complexes have been identified as API5-interacting protein partners, suggesting that API5 may act as a scaffold for multiprotein complexes. API5 exists as a monomer, and the functionally important heptad leucine repeat does not exhibit the predicted a dimeric leucine zipper. Additionally, Lys-251, which can be acetylated in cells, plays important roles in the inhibition of apoptosis under serum deprivation conditions. The acetylation of this lysine also affects the stability of API5 in cells.

Original languageEnglish
Pages (from-to)10727-10737
Number of pages11
JournalJournal of Biological Chemistry
Volume287
Issue number14
DOIs
Publication statusPublished - 2012 Mar 30

Fingerprint

Apoptosis
Proteins
Armadillos
Multiprotein Complexes
Leucine Zippers
Acetylation
Apoptosis Regulatory Proteins
Terminal Repeat Sequences
Scaffolds
Leucine
Lysine
Monomers
Crystal structure
Cells
Serum
Neoplasms

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Han, B. G., Kim, K. H., Lee, S. J., Jeong, K. C., Cho, J. W., Noh, K. H., ... Lee, B. I. (2012). Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. Journal of Biological Chemistry, 287(14), 10727-10737. https://doi.org/10.1074/jbc.M111.317594

Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. / Han, Byeong Gu; Kim, Kyoung Hoon; Lee, Sang Jae; Jeong, Kyung Chae; Cho, Jea Won; Noh, Kyung Hee; Kim, Tae Woo; Kim, Soon Jong; Yoon, Hye Jin; Suh, Se Won; Lee, Sangho; Lee, Byung Il.

In: Journal of Biological Chemistry, Vol. 287, No. 14, 30.03.2012, p. 10727-10737.

Research output: Contribution to journalArticle

Han, BG, Kim, KH, Lee, SJ, Jeong, KC, Cho, JW, Noh, KH, Kim, TW, Kim, SJ, Yoon, HJ, Suh, SW, Lee, S & Lee, BI 2012, 'Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules', Journal of Biological Chemistry, vol. 287, no. 14, pp. 10727-10737. https://doi.org/10.1074/jbc.M111.317594
Han, Byeong Gu ; Kim, Kyoung Hoon ; Lee, Sang Jae ; Jeong, Kyung Chae ; Cho, Jea Won ; Noh, Kyung Hee ; Kim, Tae Woo ; Kim, Soon Jong ; Yoon, Hye Jin ; Suh, Se Won ; Lee, Sangho ; Lee, Byung Il. / Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 14. pp. 10727-10737.
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