Insights into the structure and protein-protein interactions of the pro-apoptotic protein ASPP2

S. Rotem, C. Katz, A. Friedler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


ASPP (apoptosis-stimulating protein of p53) 2 is a pro-apoptotic protein that stimulates the p53-mediated apoptotic response. Here, we provide an overview of the structure and protein-protein interactions of ASPP2. The C-terminus of ASPP2 contains Ank (ankyrin) repeats and an SH3 domain (Src homology 3 domain). The Ank-SH3 domains mediate interactions between ASPP2 and numerous proteins involved in apoptosis such as p53 and Bcl-2. The proline-rich domain of ASPP2 is unfolded in its native state, but was not shown to mediate intermolecular interactions. Instead, it makes an intramolecular domain-domain interaction with the Ank-SH3 C-terminal domains of ASPP2. This intramolecular interaction between the unstructured proline-rich domain and the structured Ank-SH3 domains in ASPP2, which is possible due to the unfolded nature of the proline-rich domain, is proposed to have an important role in regulating the intermolecular interactions of ASPP2 with its partner proteins.

Original languageAmerican English
Pages (from-to)966-969
Number of pages4
JournalBiochemical Society Transactions
Issue number5
StatePublished - Nov 2007


  • Apoptosis-stirnulating proteins of p53 (ASPP)
  • Biophysics
  • Natively unfolded protein
  • Proline-rich domain
  • Protein-protein interaction
  • p53-mediated apoptosis


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