Evidence that HAX-1 is an interleukin-1α N-terminal binding protein

Huali Yin, Hideo Morioka, Christine A. Towle, Marc Vidal, Takeshi Watanabe, Lawrence Weissbach

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


During studies aimed at understanding the function of the N-terminal peptide of interleukin-1α (IL-1 NTP, amino acids 1-112), which is liberated from the remainder of IL-1α during intracellular processing, we identified by yeast two-hybrid analysis a putative interacting protein previously designated as HAX-1. In vitro binding studies and transient transfection experiments confirmed that HAX-1 can associate with the IL-1 NTP. HAX-1 was first identified as a protein that associates with HS1, a target of non-receptor protein tyrosine kinases within haematopoietic cells. Recent data have also revealed interactions between HAX-1 and three disparate proteins, polycystin-2 (derived from the PKD2 gene), a protein linked to polycystic kidney disease, cortactin, and Epstein-Barr virus nuclear antigen leader protein (EBNA-LP). Sequence analysis of different HAX-1 binding domains revealed a putative consensus binding motif that is present in various intracellular proteins. Overlapping peptides comprising the IL-1 NTP were synthesized, and binding experiments revealed that discrete peptides were capable of interacting with HAX-1. HAX-1 may serve to retain the IL-1 NTP in the cytoplasm, and complex formation between the IL-1 NTP and HAX-1 may play a role in motility and/or adhesion of cells.

Original languageEnglish
Pages (from-to)122-137
Number of pages16
Issue number3
Publication statusPublished - 2001 Aug 7
Externally publishedYes


  • HAX-1
  • In vitro binding
  • Interleukin-1α
  • Intracrine signalling
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Hematology
  • Molecular Biology


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