DataVXACS NanoPaper
journal article·2020-10-27Open access

Nanotopography Enhances Dynamic Remodeling of Tight Junction Proteins through Cytosolic Liquid Complexes

Xiao Huang, Xiaoyu Shi, Mollie Eva Hansen, Initha Setiady, Cameron L. Nemeth, Anna Celli, Bo Huang, Theodora Mauro, Michael Koval, Tejal A. Desai

ACS Nano· Volume 14· Issue 10
Publisher pageOpen full text
Source abstract

Abstract

Nanotopographic materials provide special biophysical stimuli that can regulate epithelial tight junctions and their barrier function. Through the use of total internal reflection fluorescence microscopy of live cells, we demonstrated that contact of synthetic surfaces with defined nanotopography at the apical surface of epithelial monolayers increased paracellular permeability of macromolecules. To monitor changes in tight junction morphology in live cells, we fluorescently tagged the scaffold protein zonula occludens-1 (ZO-1) through CRISPR/Cas9-based gene editing to enable live cell tracking of ZO-1 expressed at physiologic levels. Contact between cells and nanostructured surfaces destabilized junction-associated ZO-1 and promoted its arrangement into highly dynamic liquid cytosolic complexes with a 1-5 μm diameter. Junction-associated ZO-1 rapidly remodeled, and we observed the direct transformation of cytosolic complexes into junction-like structures. Claudin-family tight junction transmembrane proteins and F-actin also were associated with these ZO-1 containing cytosolic complexes. These data suggest that these cytosolic structures are important intermediates formed in response to nanotopographic cues that facilitate rapid tight junction remodeling in order to regulate paracellular permeability.
Source: openalex_inverted_index · Quality: baseline

Research context

PolymersNanomaterials

OpenAlex topics: Barrier Structure and Function Studies · S100 Proteins and Annexins · Connexins and lens biology

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, California 94158, United States

Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California 94158, United States

Department of Developmental and Cell Biology, University of California, Irvine, Irvine, California 92697, United States

UC Berkeley-UCSF Graduate Program in Bioengineering, University of California, San Francisco, San Francisco, California 94158, United States

Department of Dermatology, University of California, San Francisco, San Francisco, California 94158, United States

Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94158, United States

Chan Zuckerberg Biohub, San Francisco, California 94158, United States

Division of Pulmonary, Allergy, and Critical Care Medicine and Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322, United States

Funding

National Institute of Biomedical Imaging and Bioengineering · National Institute of General Medical Sciences · Chan Zuckerberg Biohub

References (42)

Show source-provided references
1. 10.1016/j.tcb.2009.12.00210.1016/j.tcb.2009.12.002 ↗
2. 10.1146/annurev-physiol-012110-14215010.1146/annurev-physiol-012110-142150 ↗
3. Anderson J. M. · Cold Spring Harb. Perspect. Biol. · 2009 · 1 · a00258410.1101/cshperspect.a002584 ↗
4. 10.1016/j.nantod.2014.04.00810.1016/j.nantod.2014.04.008 ↗
5. 10.1083/jcb.20071116510.1083/jcb.200711165 ↗
6. 10.1016/j.jconrel.2015.07.03310.1016/j.jconrel.2015.07.033 ↗
7. 10.1007/s10544-019-0394-910.1007/s10544-019-0394-9 ↗
8. 10.1038/s41551-019-0465-510.1038/s41551-019-0465-5 ↗
9. 10.1021/nl303779910.1021/nl3037799 ↗
10. 10.1021/nl504829f10.1021/nl504829f ↗
11. 10.1016/j.yexcr.2017.03.06510.1016/j.yexcr.2017.03.065 ↗
12. 10.1083/jcb.134.4.103110.1083/jcb.134.4.1031 ↗
13. 10.1177/221106821456102510.1177/2211068214561025 ↗
14. 10.1186/s13036-018-0108-510.1186/s13036-018-0108-5 ↗
15. 10.1038/labinvest.2012.15910.1038/labinvest.2012.159 ↗
16. 10.1007/s11095-019-2712-610.1007/s11095-019-2712-6 ↗
17. 10.1016/S0169-409X(00)00128-910.1016/S0169-409X(00)00128-9 ↗
18. 10.1242/jcs.05621810.1242/jcs.056218 ↗
19. 10.1074/jbc.RA118.00390810.1074/jbc.RA118.003908 ↗
20. 10.1074/jbc.273.45.2974510.1074/jbc.273.45.29745 ↗
21. 10.1242/jcs.11339910.1242/jcs.113399 ↗
22. 10.1073/pnas.090886910710.1073/pnas.0908869107 ↗
23. 10.1016/j.cub.2017.11.01410.1016/j.cub.2017.11.014 ↗
24. 10.1016/j.devcel.2020.07.02210.1016/j.devcel.2020.07.022 ↗
25. 10.1016/j.cell.2019.10.00610.1016/j.cell.2019.10.006 ↗
26. McCarthy K. M. · J. Cell Sci. · 2000 · 113 · 338710.1242/jcs.113.19.3387 ↗
27. 10.1016/j.cell.2019.10.01110.1016/j.cell.2019.10.011 ↗
28. 10.1016/j.bbrc.2009.02.00510.1016/j.bbrc.2009.02.005 ↗
29. 10.1016/j.biomaterials.2012.09.05110.1016/j.biomaterials.2012.09.051 ↗
30. 10.1007/s00418-002-0398-y10.1007/s00418-002-0398-y ↗
31. 10.3791/5804110.3791/58041 ↗
32. 10.1152/ajplung.00299.201010.1152/ajplung.00299.2010 ↗
33. 10.1038/s41556-018-0234-910.1038/s41556-018-0234-9 ↗
34. 10.1016/j.cell.2019.04.03710.1016/j.cell.2019.04.037 ↗
35. 10.1016/j.bbamem.2020.18333910.1016/j.bbamem.2020.183339 ↗
36. 10.1146/annurev-cellbio-100913-01332510.1146/annurev-cellbio-100913-013325 ↗
37. 10.1038/s41401-020-0470-y10.1038/s41401-020-0470-y ↗
38. 10.1016/j.biomaterials.2018.09.01510.1016/j.biomaterials.2018.09.015 ↗
39. 10.1002/adma.20180237310.1002/adma.201802373 ↗
40. 10.1063/1.500037710.1063/1.5000377 ↗
41. 10.1063/1.493667210.1063/1.4936672 ↗
42. 10.1101/85811810.1101/858118 ↗