التفاصيل البيبلوغرافية
| العنوان: |
The occludin and ZO-1 complex, defined by small angle X-ray scattering and NMR, has implications for modulating tight junction permeability. |
| المؤلفون: |
Tash, Brian R., Bewley, Maria C., Russo, Mariano, Keil, Jason M., Griffin, Kathleen A., Sundstrom, Jeffrey M., Antonetti, David A., Tian, Fang, Flanagan, John M. |
| المصدر: |
Proceedings of the National Academy of Sciences of the United States of America; 7/3/2012, Vol. 109 Issue 27, p10855-10860, 6p |
| مصطلحات موضوعية: |
X-ray scattering, NUCLEAR magnetic resonance spectroscopy, PERMEABILITY, MOLECULAR dynamics, MOLECULAR structure, MEMBRANE proteins, GENETIC mutation |
| مستخلص: |
Tight junctions (TJs) are dynamic cellular structures that are critical for compartmentalizing environments within tissues and regulating transport of small molecules, ions, and fluids. Phosphoryla-tion-dependent binding of the transmembrane protein occludin to the structural organizing protein ZO-1 contributes to the regulation of barrier properties; however, the details of their interaction are controversial. Using small angle X-ray scattering (SAXS), NMR chemical shift perturbation, cross-saturation, in vitro binding, and site-directed mutagenesis experiments, we define the interface between the ZO-1 PDZ3-SH3-U5-GuK (PSG) and occludin coiled-coil (CC) domains. The interface is comprised of basic residues in PSG and an acidic region in CC. Complex formation is blocked by a peptide (REESEEYM) that corresponds to CC residues 468-475 and includes a previously uncharacterized phosphosite, with the phos-phorylated version having a larger effect. Furthermore, mutation of E470 and E472 reduces cell border localization of occludin. Together, these results localize the interaction to an acidic region in CC and a predominantly basic helix V within the ZO-1 GuK domain. This model has important implications for the phosphor-ylation-dependent regulation of the occludin:ZO-1 complex. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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