Derek-John Atkins

Publications of Derek-John Atkins

• Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo.

  Authors: Christiane Rothkegel, Peter M Schmidt, Derek-John Atkins, Linda Sarah Hoffmann, Harald H H W Schmidt, Henning Schröder, Johannes-Peter Stasch

  Molecular pharmacology. 12/2007; 72(5):1181-90.

  The ubiquitously expressed nitric oxide (NO) receptor soluble guanylate cyclase (sGC) plays a key role in signal transduction. Binding of NO to the N-terminal prosthetic heme moiety of sGC results inThe ubiquitously expressed nitric oxide (NO) receptor soluble guanylate cyclase (sGC) plays a key role in signal transduction. Binding of NO to the N-terminal prosthetic heme moiety of sGC results in approximately 200-fold activation of the enzyme and an increased conversion of GTP into the second messenger cGMP. sGC exists as a heterodimer the dimerization of which is mediated mainly by the central region of the enzyme. In the present work, we constructed deletion mutants within the predicted dimerization region of the sGC alpha(1)- and beta(1)-subunit to precisely map the sequence segments crucial for subunit dimerization. To track mutation-induced alterations of sGC dimerization, we used a bimolecular fluorescence complementation approach that allows visualizing sGC heterodimerization in a noninvasive manner in living cells. Our study suggests that segments spanning amino acids alpha(1)363-372, alpha(1)403-422, alpha(1)440-459, beta(1)212-222, beta(1)304-333, beta(1)344-363, and beta(1)381-400 within the predicted dimerization region are involved in the process of heterodimerization and therefore in the expression of functional sGC.

• Insights into activation and dimerization of soluble guanylate cyclase

  Authors: Christiane Rothkegel, Peter Schmidt, Derek-John Atkins, Friederike Stoll, Henning Schröder, Harald Schmidt, Johannes-Peter Stasch

  BMC Pharmacology. 01/2007;