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Biophysical analysis of the dynamics of calmodulin interactions with neurogranin and Ca2+/calmodulin-dependent kinase II
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC. Beactica AB, Uppsala, Sweden.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.ORCID iD: 0000-0002-1135-2744
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC. Uppsala University, Science for Life Laboratory, SciLifeLab. Beactica AB, Uppsala, Sweden.ORCID iD: 0000-0003-2728-0340
2017 (English)In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 30, p. 1-11, article id e2621Article in journal (Refereed) Published
Abstract [en]

Calmodulin (CaM) functions depend on interactions with CaM-binding proteins, regulated by Ca2+. Induced structural changes influence the affinity, kinetics, and specificities of the interactions. The dynamics of CaM interactions with neurogranin (Ng) and the CaM-binding region of Ca2+/calmodulin-dependent kinase II (CaMKII290-309) have been studied using biophysical methods. These proteins have opposite Ca2+ dependencies for CaM binding. Surface plasmon resonance biosensor analysis confirmed that Ca2+ and CaM interact very rapidly, and with moderate affinity (KDSPR=3M). Calmodulin-CaMKII290-309 interactions were only detected in the presence of Ca2+, exhibiting fast kinetics and nanomolar affinity (KDSPR7.1nM). The CaM-Ng interaction had higher affinity under Ca2+-depleted (KDSPR480nM,3.4x105M-1s-1 and k(-1) = 1.6 x 10(-1)s(-1)) than Ca2+-saturated conditions (KDSPR19M). The IQ motif of Ng (Ng(27-50)) had similar affinity for CaM as Ng under Ca2+-saturated conditions (KDSPR=14M), but no interaction was seen under Ca2+-depleted conditions. Microscale thermophoresis using fluorescently labeled CaM confirmed the surface plasmon resonance results qualitatively, but estimated lower affinities for the Ng (KDMST890nM) and CaMKII290-309(KDMST190nM) interactions. Although CaMKII290-309 showed expected interaction characteristics, they may be different for full-length CaMKII. The data for full-length Ng, but not Ng(27-50), agree with the current model on Ng regulation of Ca2+/CaM signaling.

Place, publisher, year, edition, pages
2017. Vol. 30, p. 1-11, article id e2621
Keywords [en]
calmodulin, calmodulin-dependent kinase, surface plasmon resonance, microscale thermophoresis, neurogranin
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:uu:diva-329023DOI: 10.1002/jmr.2621ISI: 000405095400006OAI: oai:DiVA.org:uu-329023DiVA, id: diva2:1138991
Funder
Swedish Research Council, D0571301Available from: 2017-09-06 Created: 2017-09-06 Last updated: 2018-02-20Bibliographically approved

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Seeger, ChristianTalibov, Vladimir ODanielson, U. Helena

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