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dc.contributor.author Smirnova, Ekaterina
dc.contributor.author Kwan, Jamie J.
dc.contributor.author Siu, Ryan
dc.contributor.author Gao, Xin
dc.contributor.author Zoidl, Georg
dc.contributor.author Demeler, Borries
dc.contributor.author Saridakis, Vivian
dc.contributor.author Donaldson, Logan W.
dc.date.accessioned 2021-09-28T22:57:21Z
dc.date.available 2021-09-28T22:57:21Z
dc.date.issued 2016
dc.identifier.citation Smirnova, E., Kwan, J. J., Siu, R., Gao, X., Zoidl, G., Demeler, B., Saridakis, V., & Donaldson, L. W. (2016). A new mode of SAM domain mediated oligomierization observed in the CASKIN2 neuronal scaffolding protein. Cell Communication and Signaling, 14(1), Article 17. https://doi.org/10.1186/s12964-016-0140-3 en_US
dc.identifier.uri https://hdl.handle.net/10133/6049
dc.description Open access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) applies en_US
dc.description.abstract CASKIN2 is a homolog of CASKIN1, a scaffolding protein that participates in a signaling network with CASK (calcium/calmodulin-dependent serine kinase). Despite a high level of homology between CASKIN2 and CASKIN1, CASKIN2 cannot bind CASK due to the absence of a CASK Interaction Domain and consequently, may have evolved undiscovered structural and functional distinctions. Results We demonstrate that the crystal structure of the Sterile Alpha Motif (SAM) domain tandem (SAM1-SAM2) oligomer from CASKIN2 is different than CASKIN1, with the minimal repeating unit being a dimer, rather than a monomer. Analytical ultracentrifugation sedimentation velocity methods revealed differences in monomer/dimer equilibria across a range of concentrations and ionic strengths for the wild type CASKIN2 SAM tandem and a structure-directed double mutant that could not oligomerize. Further distinguishing CASKIN2 from CASKIN1, EGFP-tagged SAM tandem proteins expressed in Neuro2a cells produced punctae that were distinct both in shape and size. Conclusions This study illustrates a new way in which neuronal SAM domains can assemble into large macromolecular assemblies that might concentrate and amplify synaptic responses. en_US
dc.language.iso en_US en_US
dc.publisher BioMed Central en_US
dc.subject Analytical ultracentrifugation en_US
dc.subject Cell signaling en_US
dc.subject Crystal structure en_US
dc.subject Neuroscience en_US
dc.subject Protein structure en_US
dc.subject Scaffold protein en_US
dc.subject CASKIN2
dc.subject Sterile Alpha Motif
dc.subject.lcsh Neurosciences
dc.subject.lcsh Nuclear magnetic resonance
dc.subject.lcsh Scaffold proteins
dc.subject.lcsh Ultracentrifugation
dc.title A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution York University en_US
dc.publisher.institution King Abdullah University of Science and Technology en_US
dc.publisher.institution University of Texas Health Science Center at San Antonio en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.url https://doi.org/10.1186/s12964-016-0140-3 en_US


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