Signaling with phosphoinositides: better than binary.
When the outside of cell is stimulated,the inside generates a flurry of signals. Phosphates are sprinkled over lipids and proteins,where they are recognized within diverse signaling pathways. The kinases that congregate beneath the cell surface to provide the phosphate tags that mediate signaling have become major targets of new wave of drug design. Phosphoinositide signaling presents a particularly intriguing network whose many mysteries are now being unlocked. Research into protein domains that specifically recognize phosphoinositides have established the ENTH, FYVE,Phox,and pleckstrin homology domains s four cornerstones of phosphoinositide signaling.
Department of Pharmacology and Molecular Biology Program, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver 80262, USA. Michael.Overduin@UCHSC.edu
M
M
Overduin
M L
ML
Cheever
T G
TG
Kutateladze
D019870:1-Phosphatidylinositol 4-Kinase / Q000378:metabolism; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000737:chemistry / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
D010716:Phosphatidylinositols; D019870:1-Phosphatidylinositol 4-Kinase; D010744:Phosphoric Monoester Hydrolases