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

Ekaterina Smirnova; Jamie J. Kwan; Ryan Siu; Xin Gao; Georg Zoidl; Borries Demeler; Vivian Saridakis; Logan W. Donaldson

doi:10.1186/s12964-016-0140-3

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

Ekaterina Smirnova, Jamie J. Kwan, Ryan Siu, Xin Gao, Georg Zoidl, Borries Demeler, Vivian Saridakis, Logan W. Donaldson

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

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.

Original language	English (US)
Journal	Cell Communication and Signaling
Volume	14
Issue number	1
DOIs	https://doi.org/10.1186/s12964-016-0140-3
State	Published - Aug 22 2016

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This work was supported by the Canadian Institutes of Health Research MOP-81250 to LWD. GZ is a Canada Research Chair in Molecular and Cellular Neuroscience. XG is supported by King Abdullah University of Science and Technology. The development of the UltraScan Science Gateway is supported by the NSF grant DAC-1339649 to BD. Supercomputer time allocations were provided through NSF grant TG-MCB070039 to BD. The Center for Analytical Ultracentrifugation of Macromolecular Assemblies at the University of Texas Health Science Center at San Antonio is supported by San Antonio Cancer Institute grant P30 CA054174.

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10.1186/s12964-016-0140-3

https://repository.kaust.edu.sa/bitstream/10754/622078/1/art3A10.11862Fs12964-016-0140-3.pdf

Cite this

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title = "A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein",

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.",

author = "Ekaterina Smirnova and Kwan, {Jamie J.} and Ryan Siu and Xin Gao and Georg Zoidl and Borries Demeler and Vivian Saridakis and Donaldson, {Logan W.}",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by the Canadian Institutes of Health Research MOP-81250 to LWD. GZ is a Canada Research Chair in Molecular and Cellular Neuroscience. XG is supported by King Abdullah University of Science and Technology. The development of the UltraScan Science Gateway is supported by the NSF grant DAC-1339649 to BD. Supercomputer time allocations were provided through NSF grant TG-MCB070039 to BD. The Center for Analytical Ultracentrifugation of Macromolecular Assemblies at the University of Texas Health Science Center at San Antonio is supported by San Antonio Cancer Institute grant P30 CA054174.",

year = "2016",

month = aug,

day = "22",

doi = "10.1186/s12964-016-0140-3",

language = "English (US)",

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journal = "Cell Communication and Signaling",

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AU - Smirnova, Ekaterina

AU - Kwan, Jamie J.

AU - Siu, Ryan

AU - Gao, Xin

AU - Zoidl, Georg

AU - Demeler, Borries

AU - Saridakis, Vivian

AU - Donaldson, Logan W.

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by the Canadian Institutes of Health Research MOP-81250 to LWD. GZ is a Canada Research Chair in Molecular and Cellular Neuroscience. XG is supported by King Abdullah University of Science and Technology. The development of the UltraScan Science Gateway is supported by the NSF grant DAC-1339649 to BD. Supercomputer time allocations were provided through NSF grant TG-MCB070039 to BD. The Center for Analytical Ultracentrifugation of Macromolecular Assemblies at the University of Texas Health Science Center at San Antonio is supported by San Antonio Cancer Institute grant P30 CA054174.

PY - 2016/8/22

Y1 - 2016/8/22

N2 - 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.

AB - 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.

UR - http://hdl.handle.net/10754/622078

UR - http://biosignaling.biomedcentral.com/articles/10.1186/s12964-016-0140-3

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SN - 1478-811X

VL - 14

JO - Cell Communication and Signaling

JF - Cell Communication and Signaling

IS - 1

ER -

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

Abstract

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

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

Abstract

Bibliographical note

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

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