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A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes

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A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes. / Grahammer, Florian; Wigge, Christoph; Schell, Christoph; Kretz, Oliver; Patrakka, Jaakko; Schneider, Simon; Klose, Martin; Arnold, Sebastian J; Habermann, Anja; Bräuniger, Ricarda; Rinschen, Markus M; Völker, Linus; Bregenzer, Andreas; Rubbenstroth, Dennis; Boerries, Melanie; Kerjaschki, Dontscho; Miner, Jeffrey H; Walz, Gerd; Benzing, Thomas; Fornoni, Alessia; Frangakis, Achilleas S; Huber, Tobias B.

In: JCI INSIGHT, Vol. 1, No. 9, 16.06.2016.

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

Harvard

Grahammer, F, Wigge, C, Schell, C, Kretz, O, Patrakka, J, Schneider, S, Klose, M, Arnold, SJ, Habermann, A, Bräuniger, R, Rinschen, MM, Völker, L, Bregenzer, A, Rubbenstroth, D, Boerries, M, Kerjaschki, D, Miner, JH, Walz, G, Benzing, T, Fornoni, A, Frangakis, AS & Huber, TB 2016, 'A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes', JCI INSIGHT, vol. 1, no. 9. https://doi.org/10.1172/jci.insight.86177

APA

Grahammer, F., Wigge, C., Schell, C., Kretz, O., Patrakka, J., Schneider, S., Klose, M., Arnold, S. J., Habermann, A., Bräuniger, R., Rinschen, M. M., Völker, L., Bregenzer, A., Rubbenstroth, D., Boerries, M., Kerjaschki, D., Miner, J. H., Walz, G., Benzing, T., ... Huber, T. B. (2016). A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes. JCI INSIGHT, 1(9). https://doi.org/10.1172/jci.insight.86177

Vancouver

Grahammer F, Wigge C, Schell C, Kretz O, Patrakka J, Schneider S et al. A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes. JCI INSIGHT. 2016 Jun 16;1(9). https://doi.org/10.1172/jci.insight.86177

Bibtex

@article{334705fdce8e41ec8fa3475c1252a98f,
title = "A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes",
abstract = "Vertebrate life critically depends on renal filtration and excretion of low molecular weight waste products. This process is controlled by a specialized cell-cell contact between podocyte foot processes: the slit diaphragm (SD). Using a comprehensive set of targeted KO mice of key SD molecules, we provided genetic, functional, and high-resolution ultrastructural data highlighting a concept of a flexible, dynamic, and multilayered architecture of the SD. Our data indicate that the mammalian SD is composed of NEPHRIN and NEPH1 molecules, while NEPH2 and NEPH3 do not participate in podocyte intercellular junction formation. Unexpectedly, homo- and heteromeric NEPHRIN/NEPH1 complexes are rarely observed. Instead, single NEPH1 molecules appear to form the lower part of the junction close to the glomerular basement membrane with a width of 23 nm, while single NEPHRIN molecules form an adjacent junction more apically with a width of 45 nm. In both cases, the molecules are quasiperiodically spaced 7 nm apart. These structural findings, in combination with the flexibility inherent to the repetitive Ig folds of NEPHRIN and NEPH1, indicate that the SD likely represents a highly dynamic cell-cell contact that forms an adjustable, nonclogging barrier within the renal filtration apparatus.",
keywords = "Journal Article",
author = "Florian Grahammer and Christoph Wigge and Christoph Schell and Oliver Kretz and Jaakko Patrakka and Simon Schneider and Martin Klose and Arnold, {Sebastian J} and Anja Habermann and Ricarda Br{\"a}uniger and Rinschen, {Markus M} and Linus V{\"o}lker and Andreas Bregenzer and Dennis Rubbenstroth and Melanie Boerries and Dontscho Kerjaschki and Miner, {Jeffrey H} and Gerd Walz and Thomas Benzing and Alessia Fornoni and Frangakis, {Achilleas S} and Huber, {Tobias B}",
year = "2016",
month = jun,
day = "16",
doi = "10.1172/jci.insight.86177",
language = "English",
volume = "1",
journal = "JCI INSIGHT",
issn = "2379-3708",
publisher = "The American Society for Clinical Investigation",
number = "9",

}

RIS

TY - JOUR

T1 - A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes

AU - Grahammer, Florian

AU - Wigge, Christoph

AU - Schell, Christoph

AU - Kretz, Oliver

AU - Patrakka, Jaakko

AU - Schneider, Simon

AU - Klose, Martin

AU - Arnold, Sebastian J

AU - Habermann, Anja

AU - Bräuniger, Ricarda

AU - Rinschen, Markus M

AU - Völker, Linus

AU - Bregenzer, Andreas

AU - Rubbenstroth, Dennis

AU - Boerries, Melanie

AU - Kerjaschki, Dontscho

AU - Miner, Jeffrey H

AU - Walz, Gerd

AU - Benzing, Thomas

AU - Fornoni, Alessia

AU - Frangakis, Achilleas S

AU - Huber, Tobias B

PY - 2016/6/16

Y1 - 2016/6/16

N2 - Vertebrate life critically depends on renal filtration and excretion of low molecular weight waste products. This process is controlled by a specialized cell-cell contact between podocyte foot processes: the slit diaphragm (SD). Using a comprehensive set of targeted KO mice of key SD molecules, we provided genetic, functional, and high-resolution ultrastructural data highlighting a concept of a flexible, dynamic, and multilayered architecture of the SD. Our data indicate that the mammalian SD is composed of NEPHRIN and NEPH1 molecules, while NEPH2 and NEPH3 do not participate in podocyte intercellular junction formation. Unexpectedly, homo- and heteromeric NEPHRIN/NEPH1 complexes are rarely observed. Instead, single NEPH1 molecules appear to form the lower part of the junction close to the glomerular basement membrane with a width of 23 nm, while single NEPHRIN molecules form an adjacent junction more apically with a width of 45 nm. In both cases, the molecules are quasiperiodically spaced 7 nm apart. These structural findings, in combination with the flexibility inherent to the repetitive Ig folds of NEPHRIN and NEPH1, indicate that the SD likely represents a highly dynamic cell-cell contact that forms an adjustable, nonclogging barrier within the renal filtration apparatus.

AB - Vertebrate life critically depends on renal filtration and excretion of low molecular weight waste products. This process is controlled by a specialized cell-cell contact between podocyte foot processes: the slit diaphragm (SD). Using a comprehensive set of targeted KO mice of key SD molecules, we provided genetic, functional, and high-resolution ultrastructural data highlighting a concept of a flexible, dynamic, and multilayered architecture of the SD. Our data indicate that the mammalian SD is composed of NEPHRIN and NEPH1 molecules, while NEPH2 and NEPH3 do not participate in podocyte intercellular junction formation. Unexpectedly, homo- and heteromeric NEPHRIN/NEPH1 complexes are rarely observed. Instead, single NEPH1 molecules appear to form the lower part of the junction close to the glomerular basement membrane with a width of 23 nm, while single NEPHRIN molecules form an adjacent junction more apically with a width of 45 nm. In both cases, the molecules are quasiperiodically spaced 7 nm apart. These structural findings, in combination with the flexibility inherent to the repetitive Ig folds of NEPHRIN and NEPH1, indicate that the SD likely represents a highly dynamic cell-cell contact that forms an adjustable, nonclogging barrier within the renal filtration apparatus.

KW - Journal Article

U2 - 10.1172/jci.insight.86177

DO - 10.1172/jci.insight.86177

M3 - SCORING: Journal article

C2 - 27430022

VL - 1

JO - JCI INSIGHT

JF - JCI INSIGHT

SN - 2379-3708

IS - 9

ER -