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A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems

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A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems. / Gödel, Markus; Ostendorf, Benjamin N; Baumer, Jessica; Weber, Katrin; Huber, Tobias B.

in: PLOS ONE, Jahrgang 8, Nr. 2, 2013, S. e57078.

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

Harvard

Gödel, M, Ostendorf, BN, Baumer, J, Weber, K & Huber, TB 2013, 'A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems', PLOS ONE, Jg. 8, Nr. 2, S. e57078. https://doi.org/10.1371/journal.pone.0057078

APA

Gödel, M., Ostendorf, B. N., Baumer, J., Weber, K., & Huber, T. B. (2013). A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems. PLOS ONE, 8(2), e57078. https://doi.org/10.1371/journal.pone.0057078

Vancouver

Gödel M, Ostendorf BN, Baumer J, Weber K, Huber TB. A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems. PLOS ONE. 2013;8(2):e57078. https://doi.org/10.1371/journal.pone.0057078

Bibtex

@article{cd139af54c824135adbb5917cb1f4cab,
title = "A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems",
abstract = "Mutations in the gene NPHS2 are the most common cause of hereditary steroid-resistant nephrotic syndrome. Its gene product, the stomatin family member protein podocin represents a core component of the slit diaphragm, a unique structure that bridges the space between adjacent podocyte foot processes in the kidney glomerulus. Dislocation and misexpression of slit diaphragm components have been described in the pathogenesis of acquired and hereditary nephrotic syndrome. However, little is known about mechanisms regulating cellular trafficking and turnover of podocin. Here, we discover a three amino acids-comprising motif regulating intracellular localization of podocin in cell culture systems. Mutations of this motif led to markedly reduced degradation of podocin. These findings give novel insight into the molecular biology of the slit diaphragm protein podocin, enabling future research to establish the biological relevance of podocin turnover and localization.",
keywords = "Animals, Cell Culture Techniques, Cell Line, Cell Membrane, Endosomes, Humans, Intracellular Signaling Peptides and Proteins, Membrane Microdomains, Membrane Proteins, Mice, Mutation, Protein Interaction Domains and Motifs, Protein Transport, Proteolysis, Journal Article, Research Support, Non-U.S. Gov't",
author = "Markus G{\"o}del and Ostendorf, {Benjamin N} and Jessica Baumer and Katrin Weber and Huber, {Tobias B}",
year = "2013",
doi = "10.1371/journal.pone.0057078",
language = "English",
volume = "8",
pages = "e57078",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "2",

}

RIS

TY - JOUR

T1 - A novel domain regulating degradation of the glomerular slit diaphragm protein podocin in cell culture systems

AU - Gödel, Markus

AU - Ostendorf, Benjamin N

AU - Baumer, Jessica

AU - Weber, Katrin

AU - Huber, Tobias B

PY - 2013

Y1 - 2013

N2 - Mutations in the gene NPHS2 are the most common cause of hereditary steroid-resistant nephrotic syndrome. Its gene product, the stomatin family member protein podocin represents a core component of the slit diaphragm, a unique structure that bridges the space between adjacent podocyte foot processes in the kidney glomerulus. Dislocation and misexpression of slit diaphragm components have been described in the pathogenesis of acquired and hereditary nephrotic syndrome. However, little is known about mechanisms regulating cellular trafficking and turnover of podocin. Here, we discover a three amino acids-comprising motif regulating intracellular localization of podocin in cell culture systems. Mutations of this motif led to markedly reduced degradation of podocin. These findings give novel insight into the molecular biology of the slit diaphragm protein podocin, enabling future research to establish the biological relevance of podocin turnover and localization.

AB - Mutations in the gene NPHS2 are the most common cause of hereditary steroid-resistant nephrotic syndrome. Its gene product, the stomatin family member protein podocin represents a core component of the slit diaphragm, a unique structure that bridges the space between adjacent podocyte foot processes in the kidney glomerulus. Dislocation and misexpression of slit diaphragm components have been described in the pathogenesis of acquired and hereditary nephrotic syndrome. However, little is known about mechanisms regulating cellular trafficking and turnover of podocin. Here, we discover a three amino acids-comprising motif regulating intracellular localization of podocin in cell culture systems. Mutations of this motif led to markedly reduced degradation of podocin. These findings give novel insight into the molecular biology of the slit diaphragm protein podocin, enabling future research to establish the biological relevance of podocin turnover and localization.

KW - Animals

KW - Cell Culture Techniques

KW - Cell Line

KW - Cell Membrane

KW - Endosomes

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Membrane Microdomains

KW - Membrane Proteins

KW - Mice

KW - Mutation

KW - Protein Interaction Domains and Motifs

KW - Protein Transport

KW - Proteolysis

KW - Journal Article

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

U2 - 10.1371/journal.pone.0057078

DO - 10.1371/journal.pone.0057078

M3 - SCORING: Journal article

C2 - 23437316

VL - 8

SP - e57078

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 2

ER -