Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR

Hye Young Cho; Ameeq Ul Mushtaq; Jin Young Lee; Dae Gyu Kim; Min Sook Seok; Minseok Jang; Byung Woo Han; Sunghoon Kim; Young Ho Jeon

doi:10.1016/j.febslet.2014.06.048

Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR

Hye Young Cho, Ameeq Ul Mushtaq, Jin Young Lee, Dae Gyu Kim, Min Sook Seok, Minseok Jang, Byung Woo Han, Sunghoon Kim, Young Ho Jeon

Department of Pharmacy

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

5 Citations (Scopus)

Abstract

Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.

Original language	English
Pages (from-to)	2851-2858
Number of pages	8
Journal	FEBS Letters
Volume	588
Issue number	17
DOIs	https://doi.org/10.1016/j.febslet.2014.06.048
Publication status	Published - 2014 Aug 25

Bibliographical note

Funding Information:
This work was supported by Global Frontier Project grants [ NRF-M1AXA002-2010-0029785 and NRF-2013M3A6A4045160 ], and funded by Ministry of Science, ICP and Future Planning (MISP) of Korea.

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2014.06.048

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title = "Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR",

abstract = "Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.",

author = "Cho, {Hye Young} and {Ul Mushtaq}, Ameeq and Lee, {Jin Young} and Kim, {Dae Gyu} and Seok, {Min Sook} and Minseok Jang and Han, {Byung Woo} and Sunghoon Kim and Jeon, {Young Ho}",

note = "Funding Information: This work was supported by Global Frontier Project grants [ NRF-M1AXA002-2010-0029785 and NRF-2013M3A6A4045160 ], and funded by Ministry of Science, ICP and Future Planning (MISP) of Korea. ",

year = "2014",

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doi = "10.1016/j.febslet.2014.06.048",

language = "English",

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T1 - Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR

AU - Cho, Hye Young

AU - Ul Mushtaq, Ameeq

AU - Lee, Jin Young

AU - Kim, Dae Gyu

AU - Seok, Min Sook

AU - Jang, Minseok

AU - Han, Byung Woo

AU - Kim, Sunghoon

AU - Jeon, Young Ho

N1 - Funding Information: This work was supported by Global Frontier Project grants [ NRF-M1AXA002-2010-0029785 and NRF-2013M3A6A4045160 ], and funded by Ministry of Science, ICP and Future Planning (MISP) of Korea.

PY - 2014/8/25

Y1 - 2014/8/25

N2 - Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.

AB - Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.

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Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

UN SDGs

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