Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor

Ucheor B. Choi; Rashek Kazi; Natalie Stenzoski; Lonnie P. Wollmuth; Vladimir N. Uversky; Mark E. Bowen

doi:10.1074/jbc.M113.477810

Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor

Ucheor B. Choi
, Rashek Kazi
, Natalie Stenzoski
, Lonnie P. Wollmuth
, Vladimir N. Uversky
, Mark E. Bowen

Stony Brook University
University of South Florida
Russian Academy of Sciences

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

34 Scopus citations

Abstract

Background: The NMDA-sensitive glutamate receptors contain disordered cytoplasmic domains that support isoformspecific signaling. Results: Proline residues dictate the conformational dynamics in disordered proteins, which were used to affect NMDA receptor activity. Conclusion: The intrinsically disordered cytoplasmic domain is involved in specific modes of NMDA receptor regulation. Significance: The underlying dynamics of protein disorder contribute to allosteric regulation.

Original language	English
Pages (from-to)	22506-22515
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M113.477810
State	Published - Aug 2 2013

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10.1074/jbc.M113.477810

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title = "Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor",

abstract = "Background: The NMDA-sensitive glutamate receptors contain disordered cytoplasmic domains that support isoformspecific signaling. Results: Proline residues dictate the conformational dynamics in disordered proteins, which were used to affect NMDA receptor activity. Conclusion: The intrinsically disordered cytoplasmic domain is involved in specific modes of NMDA receptor regulation. Significance: The underlying dynamics of protein disorder contribute to allosteric regulation.",

author = "Choi, \{Ucheor B.\} and Rashek Kazi and Natalie Stenzoski and Wollmuth, \{Lonnie P.\} and Uversky, \{Vladimir N.\} and Bowen, \{Mark E.\}",

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AU - Choi, Ucheor B.

AU - Kazi, Rashek

AU - Stenzoski, Natalie

AU - Wollmuth, Lonnie P.

AU - Uversky, Vladimir N.

AU - Bowen, Mark E.

PY - 2013/8/2

Y1 - 2013/8/2

N2 - Background: The NMDA-sensitive glutamate receptors contain disordered cytoplasmic domains that support isoformspecific signaling. Results: Proline residues dictate the conformational dynamics in disordered proteins, which were used to affect NMDA receptor activity. Conclusion: The intrinsically disordered cytoplasmic domain is involved in specific modes of NMDA receptor regulation. Significance: The underlying dynamics of protein disorder contribute to allosteric regulation.

AB - Background: The NMDA-sensitive glutamate receptors contain disordered cytoplasmic domains that support isoformspecific signaling. Results: Proline residues dictate the conformational dynamics in disordered proteins, which were used to affect NMDA receptor activity. Conclusion: The intrinsically disordered cytoplasmic domain is involved in specific modes of NMDA receptor regulation. Significance: The underlying dynamics of protein disorder contribute to allosteric regulation.

UR - https://www.scopus.com/pages/publications/84881261693

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DO - 10.1074/jbc.M113.477810

M3 - Article

C2 - 23782697

AN - SCOPUS:84881261693

SN - 0021-9258

VL - 288

SP - 22506

EP - 22515

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 31

ER -

Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor

Abstract

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