2013
DOI: 10.1007/s00216-013-7358-3
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Structural insights into calmodulin/adenylyl cyclase 8 interaction

Abstract: Calmodulin (CaM) is a highly conserved intracellular Ca(2+)-binding protein that exerts important functions in many cellular processes. Prominent examples of CaM-regulated proteins are adenylyl cyclases (ACs), which synthesize cAMP as a central second messenger. The interaction of ACs with CaM represents the link between Ca(2+)-signaling and cAMP-signaling pathways. Thereby, different AC isoforms stimulated by CaM, comprise diverse mechanisms of regulation by the Ca(2+) sensor. To extend the structural informa… Show more

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Cited by 17 publications
(25 citation statements)
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“…There are a large number of commercially available linkers possessing different properties including spacer length, target functional group, cleavability, and solubility. Sinz et al have used XL-MS to characterize the structure of the p53 tetramer (Arlt et al, 2017), investigated the interaction network of human protein kinase D2 within the subcellular proteins (Haupl, Ihling, & Sinz, 2016), and have monitored structural changes in calmodulin upon complexation (Herbst et al, 2013). (Hermanson, 2013).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…There are a large number of commercially available linkers possessing different properties including spacer length, target functional group, cleavability, and solubility. Sinz et al have used XL-MS to characterize the structure of the p53 tetramer (Arlt et al, 2017), investigated the interaction network of human protein kinase D2 within the subcellular proteins (Haupl, Ihling, & Sinz, 2016), and have monitored structural changes in calmodulin upon complexation (Herbst et al, 2013). (Hermanson, 2013).…”
Section: Introductionmentioning
confidence: 99%
“…Rappsilber et al have utilized crosslinking-mass spectrometry (XL-MS) to identify the structures of two human coiled-coil complexes, the NDEL1 homodimer (38 kDa), and the NDC80 heterotetramer (176 kDa; Maiolica et al, 2007). Sinz et al have used XL-MS to characterize the structure of the p53 tetramer (Arlt et al, 2017), investigated the interaction network of human protein kinase D2 within the subcellular proteins (Haupl, Ihling, & Sinz, 2016), and have monitored structural changes in calmodulin upon complexation (Herbst et al, 2013).…”
Section: Introductionmentioning
confidence: 99%
“…have the same reactive group on either end. However, heterobifunctional cross-linkers are also used in the field, for example 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC)[1215] or succinimidyl 4,4’-azipentanoate (SDA)[1521]. It is unclear how far these cross-linker choices affect FDR estimation as they do link different amino acids and consequently one has to consider different search spaces.…”
Section: Introductionmentioning
confidence: 99%
“…Alternatively, five of the seven compounds tested were more potent against RGS14 (two cysteines) than RGS4 (four cysteines), but RGS18, which also contains two cysteines was refractory to inhibition. Additionally, RGS17 only contains one cysteine and RGS8 harbors an IQ-like motif, and its interaction with CaM is dependent upon Ca 2+ binding to the N-terminal lobe of CaM [74,82]. As the CaM-interacting intracellular regions of AC1 and AC8 are divergent, there is hope that small molecule PPI inhibitors may be able to selectively inhibit the interaction between CaM and AC8 or AC1.…”
Section: Discussionmentioning
confidence: 99%
“…The fluorescent probes selected were peptides corresponding to the Nt and C2b CaM-binding domains of AC8. Peptides from these areas were shown to bind CaM in a Ca 2+ -dependent manner [74,82]. These peptides were N-terminally labeled with the fluorescent dye Cy5.…”
Section: Development Of a Biochemical Assay To Detect Ac8-cam Interacmentioning
confidence: 99%