creators_name: Boradia, Vishant Mahendra
creators_name: Raje, Manoj
creators_name: Raje, Chaaya Iyengar
type: article
datestamp: 2015-02-09 09:49:23
lastmod: 2015-02-09 09:49:23
metadata_visibility: show
title: Protein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
ispublished: pub
keywords: Biochem Soc Trans
abstract: Iron is essential for the survival of both prokaryotic and eukaryotic organisms. It functions as a cofactor for several vital enzymes and iron deprivation is fatal to cells. However, at the same time, excess amounts of iron are also toxic to cells due to the formation of free radicals via the Fenton reaction. As a consequence of its double-edged behaviour, the uptake and regulation of iron involves an intricate balance of acquisition, trafficking, recycling and shuffling between various tissues and organs. This is accomplished by differential regulation of genes involving numerous proteins and enzymes. Several of the proteins identified in these processes, such as glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aconitase and lactoferrin (Lf), possess multiple functions within the cell. Such proteins are referred to as moonlighting or multifunctional proteins, whereby proteins initially thought to possess a single well-established function have subsequently been discovered to exhibit alternative functions. In many cases, these multiple functions are conserved across species.
date: 2014-12
date_type: published
publication: Biochemical Society transactions
volume: 42
number: 6
publisher:     London : Portland Press On The Behalf Of The Biochemical Society
pagerange: 1796-801
refereed: TRUE
issn: 1470-8752
official_url: http://www.biochemsoctrans.org/bst/042/1796/bst0421796.htm
citation:   Boradia, Vishant Mahendra and Raje, Manoj and Raje, Chaaya Iyengar  (2014) Protein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH).  Biochemical Society transactions, 42 (6).  pp. 1796-801.  ISSN 1470-8752