Review abstract


Nature Methods 2, 17 - 25 (2005)
Published online: 21 December 2004 | doi:10.1038/nmeth731

Kinomics: methods for deciphering the kinome

Sam A Johnson1 & Tony Hunter1


Phosphorylation by protein kinases is the most widespread and well-studied signaling mechanism in eukaryotic cells. Phosphorylation can regulate almost every property of a protein and is involved in all fundamental cellular processes. Cataloging and understanding protein phosphorylation is no easy task: many kinases may be expressed in a cell, and one-third of all intracellular proteins may be phosphorylated, representing as many as 20,000 distinct phosphoprotein states. Defining the kinase complement of the human genome, the kinome, has provided an excellent starting point for understanding the scale of the problem. The kinome consists of 518 kinases, and every active protein kinase phosphorylates a distinct set of substrates in a regulated manner. Deciphering the complex network of phosphorylation-based signaling is necessary for a thorough and therapeutically applicable understanding of the functioning of a cell in physiological and pathological states. We review contemporary techniques for identifying physiological substrates of the protein kinases and studying phosphorylation in living cells.

Top
  1. Molecular and Cell Biology Laboratory, Salk Institute, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.

Correspondence to: Tony Hunter1 e-mail: hunter@salk.edu



MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

REVIEWS

Interpreting the protein language using proteomics

Nature Reviews Molecular Cell Biology Review (01 Jun 2006)

See all 3 matches for Reviews

NEWS AND VIEWS

Phosphoproteomics finds its timing

Nature Biotechnology News and Views (01 Sep 2004)


Extra navigation

Subscribe to Nature Methods

Subscribe

Search PubMed for

natureevents

ADVERTISEMENT