New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling

Research output: Contribution to journal › Journal article › Research › peer-review

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New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling. / Choi, Youngsil; Yun, Ji-Hye; Yoo, Jiho; Lee, Inhwan; Kim, Heeyoun; Son, Hye-Nam; Kim, In-San; Yoon, Ho Sup; Zimmermann, Pascale; Couchman, John R; Cho, Hyun-Soo; Oh, Eok-Soo; Lee, Weontae.

In: Scientific Reports, Vol. 6, 36818, 10.11.2016.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Choi, Y, Yun, J-H, Yoo, J, Lee, I, Kim, H, Son, H-N, Kim, I-S, Yoon, HS, Zimmermann, P, Couchman, JR, Cho, H-S, Oh, E-S & Lee, W 2016, 'New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling', Scientific Reports, vol. 6, 36818. https://doi.org/10.1038/srep36818

APA

Choi, Y., Yun, J-H., Yoo, J., Lee, I., Kim, H., Son, H-N., Kim, I-S., Yoon, H. S., Zimmermann, P., Couchman, J. R., Cho, H-S., Oh, E-S., & Lee, W. (2016). New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling. Scientific Reports, 6, [36818]. https://doi.org/10.1038/srep36818

Vancouver

Choi Y, Yun J-H, Yoo J, Lee I, Kim H, Son H-N et al. New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling. Scientific Reports. 2016 Nov 10;6. 36818. https://doi.org/10.1038/srep36818

Author

Choi, Youngsil ; Yun, Ji-Hye ; Yoo, Jiho ; Lee, Inhwan ; Kim, Heeyoun ; Son, Hye-Nam ; Kim, In-San ; Yoon, Ho Sup ; Zimmermann, Pascale ; Couchman, John R ; Cho, Hyun-Soo ; Oh, Eok-Soo ; Lee, Weontae. / New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling. In: Scientific Reports. 2016 ; Vol. 6.

Bibtex

@article{058345a5f213434a9fb6a22614f9d459,
title = "New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling",
abstract = "The PDZ domain-containing scaffold protein, syntenin-1, binds to the transmembrane proteoglycan, syndecan-4, but the molecular mechanism/function of this interaction are unknown. Crystal structure analysis of syntenin-1/syndecan-4 cytoplasmic domains revealed that syntenin-1 forms a symmetrical pair of dimers anchored by a syndecan-4 dimer. The syndecan-4 cytoplasmic domain is a compact intertwined dimer with a symmetrical clamp shape and two antiparallel strands forming a cavity within the dimeric twist. The PDZ2 domain of syntenin-1 forms a direct antiparallel interaction with the syndecan-4 cytoplasmic domain, inhibiting the functions of syndecan-4 such as focal adhesion formation. Moreover, C-terminal region of syntenin-1 reveals an essential role for enhancing the molecular homodimerization. Mutation of key syntenin-1 residues involved in the syndecan-4 interaction or homodimer formation abolishes the inhibitory function of syntenin-1, as does deletion of the homodimerization-related syntenin-1 C-terminal domain. Syntenin-1, but not dimer-formation-incompetent mutants, rescued the syndecan-4-mediated inhibition of migration and pulmonary metastasis by B16F10 cells. Therefore, we conclude that syntenin-1 negatively regulates syndecan-4 function via oligomerization and/or syndecan-4 interaction, impacting cytoskeletal organization and cell migration.",
author = "Youngsil Choi and Ji-Hye Yun and Jiho Yoo and Inhwan Lee and Heeyoun Kim and Hye-Nam Son and In-San Kim and Yoon, {Ho Sup} and Pascale Zimmermann and Couchman, {John R} and Hyun-Soo Cho and Eok-Soo Oh and Weontae Lee",
year = "2016",
month = nov,
day = "10",
doi = "10.1038/srep36818",
language = "English",
volume = "6",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling

AU - Choi, Youngsil

AU - Yun, Ji-Hye

AU - Yoo, Jiho

AU - Lee, Inhwan

AU - Kim, Heeyoun

AU - Son, Hye-Nam

AU - Kim, In-San

AU - Yoon, Ho Sup

AU - Zimmermann, Pascale

AU - Couchman, John R

AU - Cho, Hyun-Soo

AU - Oh, Eok-Soo

AU - Lee, Weontae

PY - 2016/11/10

Y1 - 2016/11/10

N2 - The PDZ domain-containing scaffold protein, syntenin-1, binds to the transmembrane proteoglycan, syndecan-4, but the molecular mechanism/function of this interaction are unknown. Crystal structure analysis of syntenin-1/syndecan-4 cytoplasmic domains revealed that syntenin-1 forms a symmetrical pair of dimers anchored by a syndecan-4 dimer. The syndecan-4 cytoplasmic domain is a compact intertwined dimer with a symmetrical clamp shape and two antiparallel strands forming a cavity within the dimeric twist. The PDZ2 domain of syntenin-1 forms a direct antiparallel interaction with the syndecan-4 cytoplasmic domain, inhibiting the functions of syndecan-4 such as focal adhesion formation. Moreover, C-terminal region of syntenin-1 reveals an essential role for enhancing the molecular homodimerization. Mutation of key syntenin-1 residues involved in the syndecan-4 interaction or homodimer formation abolishes the inhibitory function of syntenin-1, as does deletion of the homodimerization-related syntenin-1 C-terminal domain. Syntenin-1, but not dimer-formation-incompetent mutants, rescued the syndecan-4-mediated inhibition of migration and pulmonary metastasis by B16F10 cells. Therefore, we conclude that syntenin-1 negatively regulates syndecan-4 function via oligomerization and/or syndecan-4 interaction, impacting cytoskeletal organization and cell migration.

AB - The PDZ domain-containing scaffold protein, syntenin-1, binds to the transmembrane proteoglycan, syndecan-4, but the molecular mechanism/function of this interaction are unknown. Crystal structure analysis of syntenin-1/syndecan-4 cytoplasmic domains revealed that syntenin-1 forms a symmetrical pair of dimers anchored by a syndecan-4 dimer. The syndecan-4 cytoplasmic domain is a compact intertwined dimer with a symmetrical clamp shape and two antiparallel strands forming a cavity within the dimeric twist. The PDZ2 domain of syntenin-1 forms a direct antiparallel interaction with the syndecan-4 cytoplasmic domain, inhibiting the functions of syndecan-4 such as focal adhesion formation. Moreover, C-terminal region of syntenin-1 reveals an essential role for enhancing the molecular homodimerization. Mutation of key syntenin-1 residues involved in the syndecan-4 interaction or homodimer formation abolishes the inhibitory function of syntenin-1, as does deletion of the homodimerization-related syntenin-1 C-terminal domain. Syntenin-1, but not dimer-formation-incompetent mutants, rescued the syndecan-4-mediated inhibition of migration and pulmonary metastasis by B16F10 cells. Therefore, we conclude that syntenin-1 negatively regulates syndecan-4 function via oligomerization and/or syndecan-4 interaction, impacting cytoskeletal organization and cell migration.

U2 - 10.1038/srep36818

DO - 10.1038/srep36818

M3 - Journal article

C2 - 27830760

VL - 6

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 36818

ER -

ID: 169361018