Supplementary Material for: A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein

Handle URI:
http://hdl.handle.net/10754/624128
Title:
Supplementary Material for: A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein
Authors:
Smirnova, Ekaterina; Kwan, Jamie; Siu, Ryan; Gao, Xin ( 0000-0002-7108-3574 ) ; Zoidl, Georg; Demeler, Borries; Saridakis, Vivian; Donaldson, Logan
Abstract:
Abstract Background 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.
KAUST Department:
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
Citation:
Smirnova, E., Kwan, J., Siu, R., Gao, X., Zoidl, G., Borries Demeler, … Donaldson, L. (2016). A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein. Figshare. https://doi.org/10.6084/m9.figshare.c.3601367
Publisher:
Figshare
Issue Date:
2016
DOI:
10.6084/m9.figshare.c.3601367
Type:
Dataset
Is Supplement To:
Smirnova E, Kwan JJ, Siu R, Gao X, Zoidl G, et al. (2016) A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein. Cell Communication and Signaling 14. Available: http://dx.doi.org/10.1186/s12964-016-0140-3.; DOI:10.1186/s12964-016-0140-3; HANDLE:http://hdl.handle.net/10754/622078
Appears in Collections:
Datasets; Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorSmirnova, Ekaterinaen
dc.contributor.authorKwan, Jamieen
dc.contributor.authorSiu, Ryanen
dc.contributor.authorGao, Xinen
dc.contributor.authorZoidl, Georgen
dc.contributor.authorDemeler, Borriesen
dc.contributor.authorSaridakis, Vivianen
dc.contributor.authorDonaldson, Loganen
dc.date.accessioned2017-06-06T07:44:32Z-
dc.date.available2017-06-06T07:44:32Z-
dc.date.created2016-12-14en
dc.date.issued2016en
dc.identifier.citationSmirnova, E., Kwan, J., Siu, R., Gao, X., Zoidl, G., Borries Demeler, … Donaldson, L. (2016). A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein. Figshare. https://doi.org/10.6084/m9.figshare.c.3601367en
dc.identifier.doi10.6084/m9.figshare.c.3601367en
dc.identifier.urihttp://hdl.handle.net/10754/624128-
dc.description.abstractAbstract Background 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
dc.publisherFigshareen
dc.rightsCC BYen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectBiophysicsen
dc.subjectBiochemistryen
dc.subjectMicrobiologyen
dc.subjectNeuroscienceen
dc.subjectPlant Biologyen
dc.titleSupplementary Material for: A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding proteinen
dc.typeDataseten
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Divisionen
kaust.authorGao, Xinen
dc.type.resourceCollectionen
dc.relation.isSupplementToSmirnova E, Kwan JJ, Siu R, Gao X, Zoidl G, et al. (2016) A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein. Cell Communication and Signaling 14. Available: http://dx.doi.org/10.1186/s12964-016-0140-3.en
dc.relation.isSupplementToDOI:10.1186/s12964-016-0140-3en
dc.relation.isSupplementToHANDLE:http://hdl.handle.net/10754/622078en
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