Research ExplorerPublicationsInteraction with podocin facilitates nephrin signaling

Interaction with podocin facilitates nephrin signaling

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Interaction with podocin facilitates nephrin signaling. / Huber, T B; Kottgen, M; Schilling, B; Walz, G; Benzing, T.

In: J BIOL CHEM, Vol. 276, No. 45, 09.11.2001, p. 41543-6.

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

Harvard

Huber, TB, Kottgen, M, Schilling, B, Walz, G & Benzing, T 2001, 'Interaction with podocin facilitates nephrin signaling', J BIOL CHEM, vol. 276, no. 45, pp. 41543-6. https://doi.org/10.1074/jbc.C100452200

APA

Huber, T. B., Kottgen, M., Schilling, B., Walz, G., & Benzing, T. (2001). Interaction with podocin facilitates nephrin signaling. J BIOL CHEM, 276(45), 41543-6. https://doi.org/10.1074/jbc.C100452200

Vancouver

Huber TB, Kottgen M, Schilling B, Walz G, Benzing T. Interaction with podocin facilitates nephrin signaling. J BIOL CHEM. 2001 Nov 9;276(45):41543-6. https://doi.org/10.1074/jbc.C100452200

Bibtex

@article{3f81d4aa961a462394351dae3b694b44,
title = "Interaction with podocin facilitates nephrin signaling",
abstract = "Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria. In addition, mice lacking CD2-associated protein (CD2AP) develop a nephrotic syndrome that resembles NPHS mutations suggesting that all three proteins are essential for the integrity of glomerular podocytes. Although the precise glomerular function of either protein remains unknown, it has been suggested that nephrin forms zipper-like interactions to maintain the structure of podocyte foot processes. We demonstrate now that nephrin is a signaling molecule, which stimulates mitogen-activated protein kinases. Nephrin-induced signaling is greatly enhanced by podocin, which binds to the cytoplasmic tail of nephrin. Mutational analysis suggests that abnormal or inefficient signaling through the nephrin-podocin complex contributes to the development of podocyte dysfunction and proteinuria.",
keywords = "Base Sequence, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Proteins, Transcription Factor AP-1, p38 Mitogen-Activated Protein Kinases, Journal Article, Research Support, Non-U.S. Gov't",
author = "Huber, {T B} and M Kottgen and B Schilling and G Walz and T Benzing",
year = "2001",
month = nov,
day = "9",
doi = "10.1074/jbc.C100452200",
language = "English",
volume = "276",
pages = "41543--6",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "45",

}

RIS

TY - JOUR

T1 - Interaction with podocin facilitates nephrin signaling

AU - Huber, T B

AU - Kottgen, M

AU - Schilling, B

AU - Walz, G

AU - Benzing, T

PY - 2001/11/9

Y1 - 2001/11/9

N2 - Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria. In addition, mice lacking CD2-associated protein (CD2AP) develop a nephrotic syndrome that resembles NPHS mutations suggesting that all three proteins are essential for the integrity of glomerular podocytes. Although the precise glomerular function of either protein remains unknown, it has been suggested that nephrin forms zipper-like interactions to maintain the structure of podocyte foot processes. We demonstrate now that nephrin is a signaling molecule, which stimulates mitogen-activated protein kinases. Nephrin-induced signaling is greatly enhanced by podocin, which binds to the cytoplasmic tail of nephrin. Mutational analysis suggests that abnormal or inefficient signaling through the nephrin-podocin complex contributes to the development of podocyte dysfunction and proteinuria.

AB - Mutations of NPHS1 or NPHS2, the genes encoding for the glomerular podocyte proteins nephrin and podocin, cause steroid-resistant proteinuria. In addition, mice lacking CD2-associated protein (CD2AP) develop a nephrotic syndrome that resembles NPHS mutations suggesting that all three proteins are essential for the integrity of glomerular podocytes. Although the precise glomerular function of either protein remains unknown, it has been suggested that nephrin forms zipper-like interactions to maintain the structure of podocyte foot processes. We demonstrate now that nephrin is a signaling molecule, which stimulates mitogen-activated protein kinases. Nephrin-induced signaling is greatly enhanced by podocin, which binds to the cytoplasmic tail of nephrin. Mutational analysis suggests that abnormal or inefficient signaling through the nephrin-podocin complex contributes to the development of podocyte dysfunction and proteinuria.

KW - Base Sequence

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Membrane Proteins

KW - Mitogen-Activated Protein Kinases

KW - Molecular Sequence Data

KW - Proteins

KW - Transcription Factor AP-1

KW - p38 Mitogen-Activated Protein Kinases

KW - Journal Article

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

U2 - 10.1074/jbc.C100452200

DO - 10.1074/jbc.C100452200

M3 - SCORING: Journal article

C2 - 11562357

VL - 276

SP - 41543

EP - 41546

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 45

ER -