Identification of protein-protein interactions of human HtrA1

Mara Campioni, Anna Severino, Lucrezia Manente, Antonio De Luca, Raffaele La Porta, Antonio Vitiello, Paola Fiore, Stefano Toldo, Enrico P. Spugnini, Marco G. Paggi, Alfonso Baldi

Research output: Contribution to journalArticlepeer-review


The human heat shock protein HtrA1, a member of the HtrA family of serine proteases, is a evolutionarily highly conserved factor which displays a widespread pattern of expression. The yeast two-hybrid technique was employed to identify new cellular proteins physically interacting with HtrA1, and thus potential targets of this serine protease. An enzymatically inactive HtrA1 point mutant, HtrA1-S328A, was generated and used as bait in a yeast two-hybrid system. Fifty-two plasmids were isolated from primary positive yeast clones. Subsequent sequencing and BLAST analysis revealed cDNAs encoding for 13 different proteins. These putative binding partners of HtrA1 appeared to be a) components of extracellular matrix; b) factors related to signal pathways, and c) unknown proteins. Among the 13 positive clones identified and reported here, it is worth of note that the interaction of HtrA1 with tubulin and collagen (extracellular matrix proteins) and with tuberin (cytoplasmic protein) is confirmed by other studies, and this further supports previous findings in which HtrA1 can be found active as an intracytoplasmic protein or as secreted protein as well.

Original languageEnglish
Pages (from-to)1493-1499
Number of pages7
JournalFrontiers in Bioscience - Elite
Volume3 E
Issue number4
Publication statusPublished - Jan 6 2011


  • Cancer
  • HtrA1
  • Protein-protein interaction
  • Two-hybrid

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Medicine(all)


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