Kinome

In molecular biology, the kinome is the ensemble of kinases that are expressed in a particular cell or present in the genome of an organism. Kinases are enzymes that catalyze phosphorylation reactions and fall into several families, e.g., those that phosphorylate the amino acids serine and threonine, those that phosphorylate tyrosine and a few border cases such as those related to MLK3 and the two LRRK proteins.

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It was long believed that serine/threonine kinases played different metabolic roles than tyrosine kinases, the former being used mainly for inducing conformational changes versus the latter being used to create structural "handles" on proteins that to enable binding by an SH2 domain. However, recent research has shown that there are specialized protein domains that bind to phosphorylated serine and threonine residues.

Kinases play critical roles in cell signaling and their activities are substantially altered in many cancer cells, providing potential targets for drug development - particularly cyclin-dependent kinases involved in regulating the cell cycle.^[1]

The kinome of rice has been cataloged and entered into a public database to aid study of phylogenetic relationships between individual kinases.^[2] Other organisms whose kinomes have been extensively studied and mapped include sea urchins^[3] and dictyostelium^[4]

References

1. ^ Workman P. (2005). Drugging the cancer kinome: progress and challenges in developing personalized molecular cancer therapeutics. Cold Spring Harb Symp Quant Biol 70:499-515. PMID 16869789
2. ^ Dardick C, Chen J, Richter T, Ouyang S, Ronald P. (2006). The Rice Kinase Database. A Phylogenomic Database for the Rice Kinome. Plant Physiol Epub. PMID 17172291
3. ^ Bradham CA, Foltz KR, Beane WS, Arnone MI, Rizzo F, Coffman JA, Mushegian A, Goel M, Morales J, Geneviere AM, Lapraz F, Robertson AJ, Kelkar H, Loza-Coll M, Townley IK, Raisch M, Roux MM, Lepage T, Gache C, McClay DR, Manning G. (2006). The sea urchin kinome: A first look. Dev Biol 300(1):180-93. PMID 17027740
4. ^ Goldberg JM, Manning G, Liu A, Fey P, Pilcher KE, Xu Y, Smith JL. (2006). The dictyostelium kinome--analysis of the protein kinases from a simple model organism. PLoS Genet 2(3):e38. PMID 16596165