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- ****************************************************
- * Phosphatidylinositol 3- and 4-kinases signatures *
- ****************************************************
-
- Phosphatidylinositol 3-kinase (PI3-kinase) (EC 2.7.1.137) [1] is an enzyme
- that phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol
- ring. The exact function of the three products of PI3-kinase - PI-3-P,
- PI-3,4-P(2) and PI-3,4,5-P(3) - is not yet known, although it is proposed that
- they function as second messengers in cell signalling. Currently, three forms
- of PI3-kinase are known:
-
- - The mammalian enzyme which is a heterodimer of a 110 Kd catalytic chain
- (p110) and an 85 Kd subunit (p85) which allows it to bind to activated
- tyrosine protein kinases.
- - Yeast TOR1/DRR1 and TOR2/DRR2 [2], PI3-kinases required for cell cycle
- activation. Both are proteins of about 280 Kd.
- - Yeast VPS34 [3], a PI3-kinase involved in vacuolar sorting and segregation.
- VPS34 is a protein of about 100 Kd.
-
- Phosphatidylinositol 4-kinase (PI4-kinase) (EC 2.7.1.-) [4] is an enzyme
- that acts on phosphatidylinositol (PI) in the first commited step in the
- production of the second messenger inositol-1,4,5,-trisphosphate. Currently
- a single form of PI4-kinase is known:
-
- - Yeast PIK1, a nuclear protein of 120 Kd.
-
- The PI3- and PI4-kinases share a well conserved domain at their C-terminal
- section; this domain seems to be distantly related to the catalytic domain of
- protein kinases [2]. We developed two signature patterns from the best
- conserved parts of this domain.
-
- -Consensus pattern: [LIVMFA]-K-x(2)-[DE](2)-[LIVM]-R-Q-[DE]-x(3)-[LIVMFY]-Q
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: S-x-A-x(3)-[LIVM]-x(2)-[FY]-[LIVM](2)-x-[LIVM]-x-D-R-H-
- x(2)-N
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] Hiles I.D., Otsu M., Volinia S., Fry M.J., Gout I., Dhand R.,
- Panayotou G., Ruiz-Larrea F., Thompson A., Totty N.F., Hsuan J.J.,
- Courtneidge S.A., Parker P.J., Waterfield M.D.
- Cell 70:419-429(1992).
- [ 2] Kunz J., Henriquez R., Schneider U., Deuter-Reinhard M., Movva N.,
- Hall M.N.
- Cell 73:585-596(1993).
- [ 3] Schu P.V., Takegawa K., Fry M.J., Stack J.H., Waterfield M.D., Emr S.D.
- Science 260:88-91(1993).
- [ 4] Garcia-Bustos J.F., Marini F., Stevenson I., Frei C., Hall M.N.
- EMBO J. 13:2352-2361(1994).
-