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Review
. 2012 May;213(2):115-22.
doi: 10.1530/JOE-11-0480. Epub 2012 Mar 8.

Roles of Ca2+ ions in the control of ChREBP nuclear translocation

Isabelle Leclerc  1 , Guy A Rutter, Gargi Meur, Nafeesa Noordeen
Affiliations
Review

Roles of Ca2+ ions in the control of ChREBP nuclear translocation

Isabelle Leclerc et al. J Endocrinol. 2012 May.

Abstract

Carbohydrate-responsive element binding protein (ChREBP (MLXIPL)) is emerging as an important mediator of glucotoxity both in the liver and in the pancreatic β-cells. Although the regulation of its nuclear translocation and transcriptional activation by glucose has been the subject of intensive research, it is still not fully understood. We have recently uncovered a novel mechanism in the excitable pancreatic β-cell where ChREBP interacts with sorcin, a penta-EF-hand Ca(2)(+)-binding protein, and is sequestered in the cytosol at low glucose concentrations. Upon stimulation with glucose and activation of Ca(2)(+) influx, or application of ATP as an intracellular Ca(2)(+)-mobilising agent, ChREBP rapidly translocates to the nucleus. In sorcin-silenced cells, ChREBP is constitutively present in the nucleus, and both glucose and Ca(2)(+) are ineffective in stimulating further ChREBP nuclear shuttling. Whether an active Ca(2)(+)-sorcin element of ChREBP activation also exists in non-excitable cells is discussed.

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