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PMID:11007757
| Citation |
Kikuchi, Y, Hirano, M, Seto, M and Takatsu, K (2000) Identification and characterization of a molecule, BAM11, that associates with the pleckstrin homology domain of mouse Btk. Int. Immunol. 12:1397-408 |
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| Abstract |
Bruton's tyrosine kinase (Btk) is required for normal B cell development and signal transduction through cell surface molecules, and its defects lead to X-linked immune deficiency in mice and X-linked agammaglobulinemia in humans. In this report, we will describe the identification and characterization of a molecule, BAM11, which binds to the pleckstrin homology domain of Btk. A sequence homology search revealed that BAM11 has 89% homology, at the amino acid level, to human LTG19/ENL, that was originally identified as one of the fusion partners involved in chromosomal translocations of 11q23, MLL/ALL-1/HRX, in leukemia cells. Deletion mutants demonstrated that the region of BAM11 required for binding to Btk was localized between amino acid residues 240 and 256. Forced expression of a truncated form of BAM11 (amino acids 246-368) inhibited IL-5-induced proliferation by 50%, whereas forced expression of full-length BAM11 in Y16 cells did not affect the IL-5 responsiveness. We have also shown that BAM11 (amino acids 246-368) inhibited the kinase activity of Btk. These results suggest that the binding of BAM11 to Btk plays a regulatory role in the Btk signal transduction pathway. A cell fractionation study and analysis using EGFP-fused Btk protein demonstrated that a proportion of Btk is present within the nucleus. |
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| Keywords |
Amino Acid Sequence; Animals; Base Sequence; Blood Proteins/metabolism; Cell Line; Interleukin-2/pharmacology; Interleukin-5/pharmacology; Mice; Molecular Sequence Data; Phosphoproteins/metabolism; Protein-Tyrosine Kinases/analysis; Protein-Tyrosine Kinases/antagonists & inhibitors; Protein-Tyrosine Kinases/metabolism; Sequence Homology, Amino Acid |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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