Bruton's tyrosine kinase
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Btk
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| Identifiers | |
| Symbol | BTK |
| HUGO | 1133 |
| Entrez | BTK |
| OMIM | 300300 |
| Other data | |
| Locus | Chr. X [1] |
Bruton's tyrosine kinase (or Btk) is a type of kinase enzyme implicated in the primary immunodeficiency disease X-linked agammaglobulinemia (XLA). Its exact mechanism of action remains unknown, but it plays a crucial role in B cell maturation as well as mast cell activation through the high-affinity IgE receptor. Patients with XLA have normal pre-B cell populations in their bone marrow but these cells fail to mature and enter the circulation. The BTK gene is located on the X chromosome.[1] At least 24 mutations of the BTK gene have been identified.
Btk contains a PH domain which binds Phosphatidylinositol (3,4,5)-trisphosphate (PIP3). PIP3 binding induces Btk to phosphorylate phospholipase C, which in turn hydrolyzes PIP2, a phosphatidylinositol, into two second messagers, inositol triphosphate (IP3) and diacylglycerol(DAG), which then go on to modulate the activity of downstream proteins during B-cell signalling.
Bruton's tyrosine kinase was discovered in 1993 and is named for Dr. Ogden Bruton, who first described XLA in 1952.[1]
[edit] Links
- UMich Orientation of Proteins in Membranes protein/pdbid-1bwn - Calculated orientation of Bruton's tyrosine kinase PH domain in membrane
[edit] References
- ^ a b X-Linked Agammaglobulinemia Patient and Family Handbook for The Primary Immune Diseases. Third Edition. 2001. Published by the Immune Deficiency Foundation.
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