Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation

Naniye Cetinbas; Helen Huang-Hobbs; Cristina Tognon; Gabriel Leprivier; Jianghong An; Steven McKinney; Mary Bowden; Connie Chow; Martin Gleave; Lawrence P. McIntosh; Poul H. Sorensen

doi:10.1074/jbc.M113.475301

Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation

Naniye Cetinbas, Helen Huang-Hobbs, Cristina Tognon, Gabriel Leprivier, Jianghong An, Steven McKinney, Mary Bowden, Connie Chow, Martin Gleave, Lawrence P. McIntosh, Poul H. Sorensen

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

14 Scopus citations

Abstract

Background: SAM domain-mediated polymerization is essential for ETV6-NTRK3 (EN)-induced cellular transformation. Results: Mutation of a salt bridge at the SAM polymer interface weakens SAM polymerization and abrogates EN transformation. Conclusion: Intermolecular electrostatic interactions are important for SAM domain polymerization and EN transformation. Significance: These studies provide further insights into the mechanisms by which ETV6-SAM domain mediates EN transformation.

Original language	English (US)
Pages (from-to)	27940-27950
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M113.475301
State	Published - Sep 27 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.475301

Cite this

Cetinbas, N., Huang-Hobbs, H., Tognon, C., Leprivier, G., An, J., McKinney, S., Bowden, M., Chow, C., Gleave, M., McIntosh, L. P., & Sorensen, P. H. (2013). Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation. Journal of Biological Chemistry, 288(39), 27940-27950. https://doi.org/10.1074/jbc.M113.475301

Cetinbas, N, Huang-Hobbs, H, Tognon, C, Leprivier, G, An, J, McKinney, S, Bowden, M, Chow, C, Gleave, M, McIntosh, LP & Sorensen, PH 2013, 'Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation', Journal of Biological Chemistry, vol. 288, no. 39, pp. 27940-27950. https://doi.org/10.1074/jbc.M113.475301

@article{618c546e45c242c888c090b49b40187f,

title = "Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation",

abstract = "Background: SAM domain-mediated polymerization is essential for ETV6-NTRK3 (EN)-induced cellular transformation. Results: Mutation of a salt bridge at the SAM polymer interface weakens SAM polymerization and abrogates EN transformation. Conclusion: Intermolecular electrostatic interactions are important for SAM domain polymerization and EN transformation. Significance: These studies provide further insights into the mechanisms by which ETV6-SAM domain mediates EN transformation.",

author = "Naniye Cetinbas and Helen Huang-Hobbs and Cristina Tognon and Gabriel Leprivier and Jianghong An and Steven McKinney and Mary Bowden and Connie Chow and Martin Gleave and McIntosh, {Lawrence P.} and Sorensen, {Poul H.}",

year = "2013",

month = sep,

day = "27",

doi = "10.1074/jbc.M113.475301",

language = "English (US)",

volume = "288",

pages = "27940--27950",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "39",

}

TY - JOUR

T1 - Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation

AU - Cetinbas, Naniye

AU - Huang-Hobbs, Helen

AU - Tognon, Cristina

AU - Leprivier, Gabriel

AU - An, Jianghong

AU - McKinney, Steven

AU - Bowden, Mary

AU - Chow, Connie

AU - Gleave, Martin

AU - McIntosh, Lawrence P.

AU - Sorensen, Poul H.

PY - 2013/9/27

Y1 - 2013/9/27

N2 - Background: SAM domain-mediated polymerization is essential for ETV6-NTRK3 (EN)-induced cellular transformation. Results: Mutation of a salt bridge at the SAM polymer interface weakens SAM polymerization and abrogates EN transformation. Conclusion: Intermolecular electrostatic interactions are important for SAM domain polymerization and EN transformation. Significance: These studies provide further insights into the mechanisms by which ETV6-SAM domain mediates EN transformation.

AB - Background: SAM domain-mediated polymerization is essential for ETV6-NTRK3 (EN)-induced cellular transformation. Results: Mutation of a salt bridge at the SAM polymer interface weakens SAM polymerization and abrogates EN transformation. Conclusion: Intermolecular electrostatic interactions are important for SAM domain polymerization and EN transformation. Significance: These studies provide further insights into the mechanisms by which ETV6-SAM domain mediates EN transformation.

UR - http://www.scopus.com/inward/record.url?scp=84884780623&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84884780623&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.475301

DO - 10.1074/jbc.M113.475301

M3 - Article

C2 - 23798677

AN - SCOPUS:84884780623

SN - 0021-9258

VL - 288

SP - 27940

EP - 27950

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 39

ER -

Mutation of the salt bridge-forming residues in the ETV6-SAM domain interface blocks ETV6-NTRK3-induced cellular transformation

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this