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NEPH1 defines a novel family of podocin interacting proteins

Standard

NEPH1 defines a novel family of podocin interacting proteins. / Sellin, Lorenz; Huber, Tobias B; Gerke, Peter; Quack, Ivo; Pavenstädt, Hermann; Walz, Gerd.

in: FASEB J, Jahrgang 17, Nr. 1, 01.2003, S. 115-7.

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

Harvard

Sellin, L, Huber, TB, Gerke, P, Quack, I, Pavenstädt, H & Walz, G 2003, 'NEPH1 defines a novel family of podocin interacting proteins', FASEB J, Jg. 17, Nr. 1, S. 115-7. https://doi.org/10.1096/fj.02-0242fje

APA

Sellin, L., Huber, T. B., Gerke, P., Quack, I., Pavenstädt, H., & Walz, G. (2003). NEPH1 defines a novel family of podocin interacting proteins. FASEB J, 17(1), 115-7. https://doi.org/10.1096/fj.02-0242fje

Vancouver

Sellin L, Huber TB, Gerke P, Quack I, Pavenstädt H, Walz G. NEPH1 defines a novel family of podocin interacting proteins. FASEB J. 2003 Jan;17(1):115-7. https://doi.org/10.1096/fj.02-0242fje

Bibtex

@article{9d78214d65f54307a9172560e853546a,
title = "NEPH1 defines a novel family of podocin interacting proteins",
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 NEPH1 develop a nephrotic syndrome that resembles NPHS mutations, suggesting that all three proteins are essential for the integrity of glomerular podocytes. Podocin interacts with the C-terminal domain of nephrin and facilitates nephrin-dependent signaling. NEPH1, a member of the immunoglobulin superfamily, is structurally related to nephrin. We report now that NEPH1 belongs to a family of three closely related proteins that interact with the C-terminal domain of podocin. All three NEPH proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of NEPH1 for podocin. NEPH1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. We conclude that NEPH1 defines a new family of podocin-binding molecules that are potential candidates for hereditary nephrotic syndromes not linked to either NPHS1 or NPHS2.",
keywords = "Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Humans, Intracellular Signaling Peptides and Proteins, Kidney, Membrane Proteins, Mice, Models, Biological, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proteins, Signal Transduction, Transcription Factor AP-1, Journal Article",
author = "Lorenz Sellin and Huber, {Tobias B} and Peter Gerke and Ivo Quack and Hermann Pavenst{\"a}dt and Gerd Walz",
year = "2003",
month = jan,
doi = "10.1096/fj.02-0242fje",
language = "English",
volume = "17",
pages = "115--7",
journal = "FASEB J",
issn = "0892-6638",
publisher = "FASEB",
number = "1",

}

RIS

TY - JOUR

T1 - NEPH1 defines a novel family of podocin interacting proteins

AU - Sellin, Lorenz

AU - Huber, Tobias B

AU - Gerke, Peter

AU - Quack, Ivo

AU - Pavenstädt, Hermann

AU - Walz, Gerd

PY - 2003/1

Y1 - 2003/1

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 NEPH1 develop a nephrotic syndrome that resembles NPHS mutations, suggesting that all three proteins are essential for the integrity of glomerular podocytes. Podocin interacts with the C-terminal domain of nephrin and facilitates nephrin-dependent signaling. NEPH1, a member of the immunoglobulin superfamily, is structurally related to nephrin. We report now that NEPH1 belongs to a family of three closely related proteins that interact with the C-terminal domain of podocin. All three NEPH proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of NEPH1 for podocin. NEPH1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. We conclude that NEPH1 defines a new family of podocin-binding molecules that are potential candidates for hereditary nephrotic syndromes not linked to either NPHS1 or NPHS2.

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 NEPH1 develop a nephrotic syndrome that resembles NPHS mutations, suggesting that all three proteins are essential for the integrity of glomerular podocytes. Podocin interacts with the C-terminal domain of nephrin and facilitates nephrin-dependent signaling. NEPH1, a member of the immunoglobulin superfamily, is structurally related to nephrin. We report now that NEPH1 belongs to a family of three closely related proteins that interact with the C-terminal domain of podocin. All three NEPH proteins share a conserved podocin-binding motif; mutation of a centrally located tyrosine residue dramatically lowers the affinity of NEPH1 for podocin. NEPH1 triggers AP-1 activation similarly to nephrin but requires the presence of Tec family kinases for efficient transactivation. We conclude that NEPH1 defines a new family of podocin-binding molecules that are potential candidates for hereditary nephrotic syndromes not linked to either NPHS1 or NPHS2.

KW - Amino Acid Sequence

KW - Animals

KW - Carrier Proteins

KW - Cell Line

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Kidney

KW - Membrane Proteins

KW - Mice

KW - Models, Biological

KW - Protein Structure, Tertiary

KW - Protein-Tyrosine Kinases

KW - Proteins

KW - Signal Transduction

KW - Transcription Factor AP-1

KW - Journal Article

U2 - 10.1096/fj.02-0242fje

DO - 10.1096/fj.02-0242fje

M3 - SCORING: Journal article

C2 - 12424224

VL - 17

SP - 115

EP - 117

JO - FASEB J

JF - FASEB J

SN - 0892-6638

IS - 1

ER -