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Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity

Standard

Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity. / Hartleben, Björn; Schweizer, Heiko; Lübben, Pauline; Bartram, Malte P; Möller, Clemens C; Herr, Ronja; Wei, Changli; Neumann-Haefelin, Elke; Schermer, Bernhard; Zentgraf, Hanswalter; Kerjaschki, Dontscho; Reiser, Jochen; Walz, Gerd; Benzing, Thomas; Huber, Tobias B.

in: J BIOL CHEM, Jahrgang 283, Nr. 34, 22.08.2008, S. 23033-8.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Hartleben, B, Schweizer, H, Lübben, P, Bartram, MP, Möller, CC, Herr, R, Wei, C, Neumann-Haefelin, E, Schermer, B, Zentgraf, H, Kerjaschki, D, Reiser, J, Walz, G, Benzing, T & Huber, TB 2008, 'Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity', J BIOL CHEM, Jg. 283, Nr. 34, S. 23033-8. https://doi.org/10.1074/jbc.M803143200

APA

Hartleben, B., Schweizer, H., Lübben, P., Bartram, M. P., Möller, C. C., Herr, R., Wei, C., Neumann-Haefelin, E., Schermer, B., Zentgraf, H., Kerjaschki, D., Reiser, J., Walz, G., Benzing, T., & Huber, T. B. (2008). Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity. J BIOL CHEM, 283(34), 23033-8. https://doi.org/10.1074/jbc.M803143200

Vancouver

Hartleben B, Schweizer H, Lübben P, Bartram MP, Möller CC, Herr R et al. Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity. J BIOL CHEM. 2008 Aug 22;283(34):23033-8. https://doi.org/10.1074/jbc.M803143200

Bibtex

@article{49e5d1f826de40d9bdd424fafe9083a5,
title = "Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity",
abstract = "The kidney filter represents a unique assembly of podocyte epithelial cells that tightly enwrap the glomerular capillaries with their foot processes and the interposed slit diaphragm. So far, very little is known about the guidance cues and polarity signals required to regulate proper development and maintenance of the glomerular filtration barrier. We now identify Par3, Par6, and atypical protein kinase C (aPKC) polarity proteins as novel Neph1-Nephrin-associated proteins. The interaction was mediated through the PDZ domain of Par3 and conserved carboxyl terminal residues in Neph1 and Nephrin. Par3, Par6, and aPKC localized to the slit diaphragm as shown in immunofluorescence and immunoelectron microscopy. Consistent with a critical role for aPKC activity in podocytes, inhibition of glomerular aPKC activity with a pseudosubstrate inhibitor resulted in a loss of regular podocyte foot process architecture. These data provide an important link between cell recognition mediated through the Neph1-Nephrin complex and Par-dependent polarity signaling and suggest that this molecular interaction is essential for establishing the three-dimensional architecture of podocytes at the kidney filtration barrier.",
keywords = "Adaptor Proteins, Signal Transducing, Animals, Cell Adhesion Molecules, Cell Cycle Proteins, Cell Polarity, Humans, Kidney Glomerulus, Membrane Proteins, Mice, Mice, Inbred C57BL, Podocytes, Protein Kinase C, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Bj{\"o}rn Hartleben and Heiko Schweizer and Pauline L{\"u}bben and Bartram, {Malte P} and M{\"o}ller, {Clemens C} and Ronja Herr and Changli Wei and Elke Neumann-Haefelin and Bernhard Schermer and Hanswalter Zentgraf and Dontscho Kerjaschki and Jochen Reiser and Gerd Walz and Thomas Benzing and Huber, {Tobias B}",
year = "2008",
month = aug,
day = "22",
doi = "10.1074/jbc.M803143200",
language = "English",
volume = "283",
pages = "23033--8",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "34",

}

RIS

TY - JOUR

T1 - Neph-Nephrin proteins bind the Par3-Par6-atypical protein kinase C (aPKC) complex to regulate podocyte cell polarity

AU - Hartleben, Björn

AU - Schweizer, Heiko

AU - Lübben, Pauline

AU - Bartram, Malte P

AU - Möller, Clemens C

AU - Herr, Ronja

AU - Wei, Changli

AU - Neumann-Haefelin, Elke

AU - Schermer, Bernhard

AU - Zentgraf, Hanswalter

AU - Kerjaschki, Dontscho

AU - Reiser, Jochen

AU - Walz, Gerd

AU - Benzing, Thomas

AU - Huber, Tobias B

PY - 2008/8/22

Y1 - 2008/8/22

N2 - The kidney filter represents a unique assembly of podocyte epithelial cells that tightly enwrap the glomerular capillaries with their foot processes and the interposed slit diaphragm. So far, very little is known about the guidance cues and polarity signals required to regulate proper development and maintenance of the glomerular filtration barrier. We now identify Par3, Par6, and atypical protein kinase C (aPKC) polarity proteins as novel Neph1-Nephrin-associated proteins. The interaction was mediated through the PDZ domain of Par3 and conserved carboxyl terminal residues in Neph1 and Nephrin. Par3, Par6, and aPKC localized to the slit diaphragm as shown in immunofluorescence and immunoelectron microscopy. Consistent with a critical role for aPKC activity in podocytes, inhibition of glomerular aPKC activity with a pseudosubstrate inhibitor resulted in a loss of regular podocyte foot process architecture. These data provide an important link between cell recognition mediated through the Neph1-Nephrin complex and Par-dependent polarity signaling and suggest that this molecular interaction is essential for establishing the three-dimensional architecture of podocytes at the kidney filtration barrier.

AB - The kidney filter represents a unique assembly of podocyte epithelial cells that tightly enwrap the glomerular capillaries with their foot processes and the interposed slit diaphragm. So far, very little is known about the guidance cues and polarity signals required to regulate proper development and maintenance of the glomerular filtration barrier. We now identify Par3, Par6, and atypical protein kinase C (aPKC) polarity proteins as novel Neph1-Nephrin-associated proteins. The interaction was mediated through the PDZ domain of Par3 and conserved carboxyl terminal residues in Neph1 and Nephrin. Par3, Par6, and aPKC localized to the slit diaphragm as shown in immunofluorescence and immunoelectron microscopy. Consistent with a critical role for aPKC activity in podocytes, inhibition of glomerular aPKC activity with a pseudosubstrate inhibitor resulted in a loss of regular podocyte foot process architecture. These data provide an important link between cell recognition mediated through the Neph1-Nephrin complex and Par-dependent polarity signaling and suggest that this molecular interaction is essential for establishing the three-dimensional architecture of podocytes at the kidney filtration barrier.

KW - Adaptor Proteins, Signal Transducing

KW - Animals

KW - Cell Adhesion Molecules

KW - Cell Cycle Proteins

KW - Cell Polarity

KW - Humans

KW - Kidney Glomerulus

KW - Membrane Proteins

KW - Mice

KW - Mice, Inbred C57BL

KW - Podocytes

KW - Protein Kinase C

KW - Journal Article

KW - Research Support, N.I.H., Extramural

KW - Research Support, Non-U.S. Gov't

U2 - 10.1074/jbc.M803143200

DO - 10.1074/jbc.M803143200

M3 - SCORING: Journal article

C2 - 18562307

VL - 283

SP - 23033

EP - 23038

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 34

ER -