Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep01392
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dc.titleStructural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin
dc.contributor.authorKumar, V.
dc.contributor.authorChichili, V.P.R.
dc.contributor.authorZhong, L.
dc.contributor.authorTang, X.
dc.contributor.authorVelazquez-Campoy, A.
dc.contributor.authorSheu, F.-S.
dc.contributor.authorSeetharaman, J.
dc.contributor.authorGerges, N.Z.
dc.contributor.authorSivaraman, J.
dc.date.accessioned2014-12-12T08:02:18Z
dc.date.available2014-12-12T08:02:18Z
dc.date.issued2013
dc.identifier.citationKumar, V., Chichili, V.P.R., Zhong, L., Tang, X., Velazquez-Campoy, A., Sheu, F.-S., Seetharaman, J., Gerges, N.Z., Sivaraman, J. (2013). Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin. Scientific Reports 3 : -. ScholarBank@NUS Repository. https://doi.org/10.1038/srep01392
dc.identifier.issn20452322
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/117164
dc.description.abstractNeuromodulin (Nm) and neurogranin (Ng) are neuron-specific substrates of protein kinase C (PKC). Their interactions with Calmodulin (CaM) are crucial for learning and memory formation in neurons. Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM. These observations explain the mechanism by which PKC-induced Ser phosphorylation blocks the association of Nm/Ng with CaM and interrupts several learning-and memory-associated functions. Moreover, the present study identified Arg as a key CaM interacting residue from Nm/Ng. This residue is crucial for CaM-mediated function, as evidenced by the inability of the Ng mutant (Arg-to-Ala) to potentiate synaptic transmission in CA1 hippocampal neurons.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/srep01392
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentNUS NANOSCIENCE & NANOTECH INITIATIVE
dc.description.doi10.1038/srep01392
dc.description.sourcetitleScientific Reports
dc.description.volume3
dc.description.page-
dc.identifier.isiut000315695900003
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