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 journalArticle

30 Citations (Scopus)

Abstract

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
JournalCytokine
Volume15
Issue number3
DOIs
Publication statusPublished - 2001 Aug 7
Externally publishedYes

Fingerprint

Interleukin-1
Carrier Proteins
Proteins
Peptides
Cortactin
Epstein-Barr Virus Nuclear Antigens
Polycystic Kidney Diseases
Cell Adhesion
Yeast
Protein-Tyrosine Kinases
Transfection
Sequence Analysis
Cytoplasm
Adhesion
Genes
Yeasts
Experiments
Cells
Amino Acids
Processing

Keywords

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

ASJC Scopus subject areas

  • Endocrinology
  • Molecular Biology
  • Immunology
  • Immunology and Allergy

Cite this

Yin, H., Morioka, H., Towle, C. A., Vidal, M., Watanabe, T., & Weissbach, L. (2001). Evidence that HAX-1 is an interleukin-1α N-terminal binding protein. Cytokine, 15(3), 122-137. https://doi.org/10.1006/cyto.2001.0891

Evidence that HAX-1 is an interleukin-1α N-terminal binding protein. / Yin, Huali; Morioka, Hideo; Towle, Christine A.; Vidal, Marc; Watanabe, Takeshi; Weissbach, Lawrence.

In: Cytokine, Vol. 15, No. 3, 07.08.2001, p. 122-137.

Research output: Contribution to journalArticle

Yin, H, Morioka, H, Towle, CA, Vidal, M, Watanabe, T & Weissbach, L 2001, 'Evidence that HAX-1 is an interleukin-1α N-terminal binding protein', Cytokine, vol. 15, no. 3, pp. 122-137. https://doi.org/10.1006/cyto.2001.0891
Yin H, Morioka H, Towle CA, Vidal M, Watanabe T, Weissbach L. Evidence that HAX-1 is an interleukin-1α N-terminal binding protein. Cytokine. 2001 Aug 7;15(3):122-137. https://doi.org/10.1006/cyto.2001.0891
Yin, Huali ; Morioka, Hideo ; Towle, Christine A. ; Vidal, Marc ; Watanabe, Takeshi ; Weissbach, Lawrence. / Evidence that HAX-1 is an interleukin-1α N-terminal binding protein. In: Cytokine. 2001 ; Vol. 15, No. 3. pp. 122-137.
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