FEBS Letters
Volume 514, Issue 1 , Pages 26-29, 6 March 2002

Elongation factor-2 kinase and its newly discovered relatives

Edited by Lev Kisselev

Department of Pharmacology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway NJ 08854, USA

Received 16 November 2001; received in revised form 29 November 2001; accepted 30 November 2001.

Abstract 

Phosphorylation of elongation factor-2 (eEF-2) by the highly specific eEF-2 kinase results in eEF-2 inactivation and, therefore, may regulate the global rate of protein synthesis in animal cells. Cloning and sequencing of eEF-2 kinase led to the discovery of a new family of protein kinases, named α-kinases, whose catalytic domains display no sequence homology to conventional eukaryotic protein kinases. Several mammalian α-kinases have recently been cloned. Two of these α-kinases, named channel-kinases 1 and 2 (ChaK1 and ChaK2) represent a new type of signaling molecules that are protein kinases fused to ion channels.

Keywords:  Elongation factor-2, Protein kinase, Protein phosphorylation, α-Kinase, Ion channel, Channel-kinase, TRP channels

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(02)02299-8

FEBS Letters
Volume 514, Issue 1 , Pages 26-29, 6 March 2002