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Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels

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Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels. / Huber, Tobias B; Schermer, Bernhard; Müller, Roman Ulrich; Höhne, Martin; Bartram, Malte; Calixto, Andrea; Hagmann, Henning; Reinhardt, Christian; Koos, Fabienne; Kunzelmann, Karl; Shirokova, Elena; Krautwurst, Dietmar; Harteneck, Christian; Simons, Matias; Pavenstädt, Hermann; Kerjaschki, Dontscho; Thiele, Christoph; Walz, Gerd; Chalfie, Martin; Benzing, Thomas.

In: P NATL ACAD SCI USA, Vol. 103, No. 46, 14.11.2006, p. 17079-86.

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

Harvard

Huber, TB, Schermer, B, Müller, RU, Höhne, M, Bartram, M, Calixto, A, Hagmann, H, Reinhardt, C, Koos, F, Kunzelmann, K, Shirokova, E, Krautwurst, D, Harteneck, C, Simons, M, Pavenstädt, H, Kerjaschki, D, Thiele, C, Walz, G, Chalfie, M & Benzing, T 2006, 'Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels', P NATL ACAD SCI USA, vol. 103, no. 46, pp. 17079-86. https://doi.org/10.1073/pnas.0607465103

APA

Huber, T. B., Schermer, B., Müller, R. U., Höhne, M., Bartram, M., Calixto, A., Hagmann, H., Reinhardt, C., Koos, F., Kunzelmann, K., Shirokova, E., Krautwurst, D., Harteneck, C., Simons, M., Pavenstädt, H., Kerjaschki, D., Thiele, C., Walz, G., Chalfie, M., & Benzing, T. (2006). Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels. P NATL ACAD SCI USA, 103(46), 17079-86. https://doi.org/10.1073/pnas.0607465103

Vancouver

Huber TB, Schermer B, Müller RU, Höhne M, Bartram M, Calixto A et al. Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels. P NATL ACAD SCI USA. 2006 Nov 14;103(46):17079-86. https://doi.org/10.1073/pnas.0607465103

Bibtex

@article{8041232c864c4a968b12997d4b036056,
title = "Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels",
abstract = "The prohibitin (PHB)-domain proteins are membrane proteins that regulate a variety of biological activities, including mechanosensation, osmotic homeostasis, and cell signaling, although the mechanism of this regulation is unknown. We have studied two members of this large protein family, MEC-2, which is needed for touch sensitivity in Caenorhabditis elegans, and Podocin, a protein involved in the function of the filtration barrier in the mammalian kidney, and find that both proteins bind cholesterol. This binding requires the PHB domain (including palmitoylation sites within it) and part of the N-terminally adjacent hydrophobic domain that attaches the proteins to the inner leaflet of the plasma membrane. By binding to MEC-2 and Podocin, cholesterol associates with ion-channel complexes to which these proteins bind: DEG/ENaC channels for MEC-2 and TRPC channels for Podocin. Both the MEC-2-dependent activation of mechanosensation and the Podocin-dependent activation of TRPC channels require cholesterol. Thus, MEC-2, Podocin, and probably many other PHB-domain proteins by binding to themselves, cholesterol, and target proteins regulate the formation and function of large protein-cholesterol supercomplexes in the plasma membrane.",
keywords = "Amino Acid Sequence, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cholesterol, Humans, Intracellular Signaling Peptides and Proteins, Ion Channels, Membrane Proteins, Mice, Molecular Sequence Data, Protein Binding, Sensitivity and Specificity, Sequence Alignment, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Huber, {Tobias B} and Bernhard Schermer and M{\"u}ller, {Roman Ulrich} and Martin H{\"o}hne and Malte Bartram and Andrea Calixto and Henning Hagmann and Christian Reinhardt and Fabienne Koos and Karl Kunzelmann and Elena Shirokova and Dietmar Krautwurst and Christian Harteneck and Matias Simons and Hermann Pavenst{\"a}dt and Dontscho Kerjaschki and Christoph Thiele and Gerd Walz and Martin Chalfie and Thomas Benzing",
year = "2006",
month = nov,
day = "14",
doi = "10.1073/pnas.0607465103",
language = "English",
volume = "103",
pages = "17079--86",
journal = "P NATL ACAD SCI USA",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "46",

}

RIS

TY - JOUR

T1 - Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels

AU - Huber, Tobias B

AU - Schermer, Bernhard

AU - Müller, Roman Ulrich

AU - Höhne, Martin

AU - Bartram, Malte

AU - Calixto, Andrea

AU - Hagmann, Henning

AU - Reinhardt, Christian

AU - Koos, Fabienne

AU - Kunzelmann, Karl

AU - Shirokova, Elena

AU - Krautwurst, Dietmar

AU - Harteneck, Christian

AU - Simons, Matias

AU - Pavenstädt, Hermann

AU - Kerjaschki, Dontscho

AU - Thiele, Christoph

AU - Walz, Gerd

AU - Chalfie, Martin

AU - Benzing, Thomas

PY - 2006/11/14

Y1 - 2006/11/14

N2 - The prohibitin (PHB)-domain proteins are membrane proteins that regulate a variety of biological activities, including mechanosensation, osmotic homeostasis, and cell signaling, although the mechanism of this regulation is unknown. We have studied two members of this large protein family, MEC-2, which is needed for touch sensitivity in Caenorhabditis elegans, and Podocin, a protein involved in the function of the filtration barrier in the mammalian kidney, and find that both proteins bind cholesterol. This binding requires the PHB domain (including palmitoylation sites within it) and part of the N-terminally adjacent hydrophobic domain that attaches the proteins to the inner leaflet of the plasma membrane. By binding to MEC-2 and Podocin, cholesterol associates with ion-channel complexes to which these proteins bind: DEG/ENaC channels for MEC-2 and TRPC channels for Podocin. Both the MEC-2-dependent activation of mechanosensation and the Podocin-dependent activation of TRPC channels require cholesterol. Thus, MEC-2, Podocin, and probably many other PHB-domain proteins by binding to themselves, cholesterol, and target proteins regulate the formation and function of large protein-cholesterol supercomplexes in the plasma membrane.

AB - The prohibitin (PHB)-domain proteins are membrane proteins that regulate a variety of biological activities, including mechanosensation, osmotic homeostasis, and cell signaling, although the mechanism of this regulation is unknown. We have studied two members of this large protein family, MEC-2, which is needed for touch sensitivity in Caenorhabditis elegans, and Podocin, a protein involved in the function of the filtration barrier in the mammalian kidney, and find that both proteins bind cholesterol. This binding requires the PHB domain (including palmitoylation sites within it) and part of the N-terminally adjacent hydrophobic domain that attaches the proteins to the inner leaflet of the plasma membrane. By binding to MEC-2 and Podocin, cholesterol associates with ion-channel complexes to which these proteins bind: DEG/ENaC channels for MEC-2 and TRPC channels for Podocin. Both the MEC-2-dependent activation of mechanosensation and the Podocin-dependent activation of TRPC channels require cholesterol. Thus, MEC-2, Podocin, and probably many other PHB-domain proteins by binding to themselves, cholesterol, and target proteins regulate the formation and function of large protein-cholesterol supercomplexes in the plasma membrane.

KW - Amino Acid Sequence

KW - Animals

KW - Caenorhabditis elegans

KW - Caenorhabditis elegans Proteins

KW - Cholesterol

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Ion Channels

KW - Membrane Proteins

KW - Mice

KW - Molecular Sequence Data

KW - Protein Binding

KW - Sensitivity and Specificity

KW - Sequence Alignment

KW - Journal Article

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

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

U2 - 10.1073/pnas.0607465103

DO - 10.1073/pnas.0607465103

M3 - SCORING: Journal article

C2 - 17079490

VL - 103

SP - 17079

EP - 17086

JO - P NATL ACAD SCI USA

JF - P NATL ACAD SCI USA

SN - 0027-8424

IS - 46

ER -