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Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3

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Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. / Paz, Aviv; Zeev-Ben-Mordehai, Tzviya; Lundqvist, Martin et al.

In: Biophysical Journal, Vol. 95, No. 4, 15.08.2008, p. 1928-1944.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Paz, A, Zeev-Ben-Mordehai, T, Lundqvist, M, Sherman, E, Mylonas, E, Weiner, KL, Haran, G, Svergun, DI, Mulder, FAA, Sussman, JL & Silman, I 2008, 'Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3', Biophysical Journal, vol. 95, no. 4, pp. 1928-1944. https://doi.org/10.1529/biophysj.107.126995

APA

Paz, A., Zeev-Ben-Mordehai, T., Lundqvist, M., Sherman, E., Mylonas, E., Weiner, K. L., Haran, G., Svergun, D. I., Mulder, F. A. A., Sussman, J. L., & Silman, I. (2008). Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal, 95(4), 1928-1944. https://doi.org/10.1529/biophysj.107.126995

CBE

Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner KL, Haran G, Svergun DI, Mulder FAA, Sussman JL, et al. 2008. Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal. 95(4):1928-1944. https://doi.org/10.1529/biophysj.107.126995

MLA

Vancouver

Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner KL et al. Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal. 2008 Aug 15;95(4):1928-1944. https://doi.org/10.1529/biophysj.107.126995

Author

Paz, Aviv ; Zeev-Ben-Mordehai, Tzviya ; Lundqvist, Martin et al. / Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. In: Biophysical Journal. 2008 ; Vol. 95, No. 4. pp. 1928-1944.

Bibtex

@article{a73716cb527f4fe4a50d19f9c9fa2beb,
title = "Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3",
abstract = "Cholinesterase-like adhesion molecules (CLAMs) are a family of neuronal cell adhesion molecules with important roles in synaptogenesis, and in maintaining structural and functional integrity of the nervous system. Our earlier study on the cytoplasmic domain of one of these CLAMs, the Drosophila protein, gliotactin, showed that it is intrinsically unstructured in vitro. Bioinformatic analysis suggested that the cytoplasmic domains of other CLAMs are also intrinsically unstructured, even though they bear no sequence homology to each other or to any known protein. In this study, we overexpress and purify the cytoplasmic domain of human neuroligin 3, notwithstanding its high sensitivity to the Escherichia coli endogenous proteases that cause its rapid degradation. Using bioinformatic analysis, sensitivity to proteases, size exclusion chromatography, fluorescence correlation spectroscopy, analytical ultracentrifugation, small angle x-ray scattering, circular dichroism, electron spin resonance, and nuclear magnetic resonance, we show that the cytoplasmic domain of human neuroligin 3 is intrinsically unstructured. However, several of these techniques indicate that it is not fully extended, but becomes significantly more extended under denaturing conditions.",
author = "Aviv Paz and Tzviya Zeev-Ben-Mordehai and Martin Lundqvist and Eilon Sherman and Efstratios Mylonas and Weiner, {K. Lev} and Gilad Haran and Svergun, {Dmitri I.} and Mulder, {F. A A} and Sussman, {Joel L.} and Israel Silman",
year = "2008",
month = aug,
day = "15",
doi = "10.1529/biophysj.107.126995",
language = "English",
volume = "95",
pages = "1928--1944",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3

AU - Paz, Aviv

AU - Zeev-Ben-Mordehai, Tzviya

AU - Lundqvist, Martin

AU - Sherman, Eilon

AU - Mylonas, Efstratios

AU - Weiner, K. Lev

AU - Haran, Gilad

AU - Svergun, Dmitri I.

AU - Mulder, F. A A

AU - Sussman, Joel L.

AU - Silman, Israel

PY - 2008/8/15

Y1 - 2008/8/15

N2 - Cholinesterase-like adhesion molecules (CLAMs) are a family of neuronal cell adhesion molecules with important roles in synaptogenesis, and in maintaining structural and functional integrity of the nervous system. Our earlier study on the cytoplasmic domain of one of these CLAMs, the Drosophila protein, gliotactin, showed that it is intrinsically unstructured in vitro. Bioinformatic analysis suggested that the cytoplasmic domains of other CLAMs are also intrinsically unstructured, even though they bear no sequence homology to each other or to any known protein. In this study, we overexpress and purify the cytoplasmic domain of human neuroligin 3, notwithstanding its high sensitivity to the Escherichia coli endogenous proteases that cause its rapid degradation. Using bioinformatic analysis, sensitivity to proteases, size exclusion chromatography, fluorescence correlation spectroscopy, analytical ultracentrifugation, small angle x-ray scattering, circular dichroism, electron spin resonance, and nuclear magnetic resonance, we show that the cytoplasmic domain of human neuroligin 3 is intrinsically unstructured. However, several of these techniques indicate that it is not fully extended, but becomes significantly more extended under denaturing conditions.

AB - Cholinesterase-like adhesion molecules (CLAMs) are a family of neuronal cell adhesion molecules with important roles in synaptogenesis, and in maintaining structural and functional integrity of the nervous system. Our earlier study on the cytoplasmic domain of one of these CLAMs, the Drosophila protein, gliotactin, showed that it is intrinsically unstructured in vitro. Bioinformatic analysis suggested that the cytoplasmic domains of other CLAMs are also intrinsically unstructured, even though they bear no sequence homology to each other or to any known protein. In this study, we overexpress and purify the cytoplasmic domain of human neuroligin 3, notwithstanding its high sensitivity to the Escherichia coli endogenous proteases that cause its rapid degradation. Using bioinformatic analysis, sensitivity to proteases, size exclusion chromatography, fluorescence correlation spectroscopy, analytical ultracentrifugation, small angle x-ray scattering, circular dichroism, electron spin resonance, and nuclear magnetic resonance, we show that the cytoplasmic domain of human neuroligin 3 is intrinsically unstructured. However, several of these techniques indicate that it is not fully extended, but becomes significantly more extended under denaturing conditions.

U2 - 10.1529/biophysj.107.126995

DO - 10.1529/biophysj.107.126995

M3 - Journal article

C2 - 18456828

AN - SCOPUS:50349090754

VL - 95

SP - 1928

EP - 1944

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 4

ER -