A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein

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dc.contributor.authorSmirnova, Ekaterina
dc.contributor.authorKwan, Jamie J.
dc.contributor.authorSiu, Ryan
dc.contributor.authorGao, Xin
dc.contributor.authorZoidl, Georg
dc.contributor.authorDemeler, Borries
dc.contributor.authorSaridakis, Vivian
dc.contributor.authorDonaldson, Logan W.
dc.date.accessioned2021-09-28T22:57:21Z
dc.date.available2021-09-28T22:57:21Z
dc.date.issued2016
dc.descriptionOpen access article. Creative Commons Attribution 4.0 International License (CC BY 4.0) appliesen_US
dc.description.abstractCASKIN2 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.description.peer-reviewYesen_US
dc.identifier.citationSmirnova, 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/s12964-016-0140-3en_US
dc.identifier.urihttps://hdl.handle.net/10133/6049
dc.language.isoen_USen_US
dc.publisherBioMed Centralen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionYork Universityen_US
dc.publisher.institutionKing Abdullah University of Science and Technologyen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1186/s12964-016-0140-3en_US
dc.subjectAnalytical ultracentrifugationen_US
dc.subjectCell signalingen_US
dc.subjectCrystal structureen_US
dc.subjectNeuroscienceen_US
dc.subjectProtein structureen_US
dc.subjectScaffold proteinen_US
dc.subjectCASKIN2
dc.subjectSterile Alpha Motif
dc.subject.lcshNeurosciences
dc.subject.lcshNuclear magnetic resonance
dc.subject.lcshScaffold proteins
dc.subject.lcshUltracentrifugation
dc.titleA new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding proteinen_US
dc.typeArticleen_US
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