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The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells

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The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells. / Yasunaga, Takayuki; Hoff, Sylvia; Schell, Christoph; Helmstädter, Martin; Kretz, Oliver; Kuechlin, Sebastian; Yakulov, Toma A; Engel, Christina; Müller, Barbara; Bensch, Robert; Ronneberger, Olaf; Huber, Tobias B; Lienkamp, Soeren S; Walz, Gerd.

In: J CELL BIOL, Vol. 211, No. 5, 07.12.2015, p. 963-73.

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

Harvard

Yasunaga, T, Hoff, S, Schell, C, Helmstädter, M, Kretz, O, Kuechlin, S, Yakulov, TA, Engel, C, Müller, B, Bensch, R, Ronneberger, O, Huber, TB, Lienkamp, SS & Walz, G 2015, 'The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells', J CELL BIOL, vol. 211, no. 5, pp. 963-73. https://doi.org/10.1083/jcb.201502043

APA

Yasunaga, T., Hoff, S., Schell, C., Helmstädter, M., Kretz, O., Kuechlin, S., Yakulov, T. A., Engel, C., Müller, B., Bensch, R., Ronneberger, O., Huber, T. B., Lienkamp, S. S., & Walz, G. (2015). The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells. J CELL BIOL, 211(5), 963-73. https://doi.org/10.1083/jcb.201502043

Vancouver

Yasunaga T, Hoff S, Schell C, Helmstädter M, Kretz O, Kuechlin S et al. The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells. J CELL BIOL. 2015 Dec 7;211(5):963-73. https://doi.org/10.1083/jcb.201502043

Bibtex

@article{e16450ccf4704cd7a5ee83c0ce650144,
title = "The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells",
abstract = "Motile cilia polarization requires intracellular anchorage to the cytoskeleton; however, the molecular machinery that supports this process remains elusive. We report that Inturned plays a central role in coordinating the interaction between cilia-associated proteins and actin-nucleation factors. We observed that knockdown of nphp4 in multiciliated cells of the Xenopus laevis epidermis compromised ciliogenesis and directional fluid flow. Depletion of nphp4 disrupted the subapical actin layer. Comparison to the structural defects caused by inturned depletion revealed striking similarities. Furthermore, coimmunoprecipitation assays demonstrated that the two proteins interact with each other and that Inturned mediates the formation of ternary protein complexes between NPHP4 and DAAM1. Knockdown of daam1, but not formin-2, resulted in similar disruption of the subapical actin web, whereas nphp4 depletion prevented the association of Inturned with the basal bodies. Thus, Inturned appears to function as an adaptor protein that couples cilia-associated molecules to actin-modifying proteins to rearrange the local actin cytoskeleton.",
keywords = "Actin Cytoskeleton, Actins, Adaptor Proteins, Signal Transducing, Animals, Basal Bodies, Cilia, Drosophila melanogaster, Epidermis, Gene Knockdown Techniques, Green Fluorescent Proteins, HEK293 Cells, Humans, Immunoprecipitation, Membrane Proteins, Microfilament Proteins, Molecular Sequence Data, Oligonucleotides, Protein Binding, Protein Structure, Tertiary, Proteins, Xenopus Proteins, Xenopus laevis, Journal Article, Research Support, Non-U.S. Gov't",
author = "Takayuki Yasunaga and Sylvia Hoff and Christoph Schell and Martin Helmst{\"a}dter and Oliver Kretz and Sebastian Kuechlin and Yakulov, {Toma A} and Christina Engel and Barbara M{\"u}ller and Robert Bensch and Olaf Ronneberger and Huber, {Tobias B} and Lienkamp, {Soeren S} and Gerd Walz",
note = "{\textcopyright} 2015 Yasunaga et al.",
year = "2015",
month = dec,
day = "7",
doi = "10.1083/jcb.201502043",
language = "English",
volume = "211",
pages = "963--73",
journal = "J CELL BIOL",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "5",

}

RIS

TY - JOUR

T1 - The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells

AU - Yasunaga, Takayuki

AU - Hoff, Sylvia

AU - Schell, Christoph

AU - Helmstädter, Martin

AU - Kretz, Oliver

AU - Kuechlin, Sebastian

AU - Yakulov, Toma A

AU - Engel, Christina

AU - Müller, Barbara

AU - Bensch, Robert

AU - Ronneberger, Olaf

AU - Huber, Tobias B

AU - Lienkamp, Soeren S

AU - Walz, Gerd

N1 - © 2015 Yasunaga et al.

PY - 2015/12/7

Y1 - 2015/12/7

N2 - Motile cilia polarization requires intracellular anchorage to the cytoskeleton; however, the molecular machinery that supports this process remains elusive. We report that Inturned plays a central role in coordinating the interaction between cilia-associated proteins and actin-nucleation factors. We observed that knockdown of nphp4 in multiciliated cells of the Xenopus laevis epidermis compromised ciliogenesis and directional fluid flow. Depletion of nphp4 disrupted the subapical actin layer. Comparison to the structural defects caused by inturned depletion revealed striking similarities. Furthermore, coimmunoprecipitation assays demonstrated that the two proteins interact with each other and that Inturned mediates the formation of ternary protein complexes between NPHP4 and DAAM1. Knockdown of daam1, but not formin-2, resulted in similar disruption of the subapical actin web, whereas nphp4 depletion prevented the association of Inturned with the basal bodies. Thus, Inturned appears to function as an adaptor protein that couples cilia-associated molecules to actin-modifying proteins to rearrange the local actin cytoskeleton.

AB - Motile cilia polarization requires intracellular anchorage to the cytoskeleton; however, the molecular machinery that supports this process remains elusive. We report that Inturned plays a central role in coordinating the interaction between cilia-associated proteins and actin-nucleation factors. We observed that knockdown of nphp4 in multiciliated cells of the Xenopus laevis epidermis compromised ciliogenesis and directional fluid flow. Depletion of nphp4 disrupted the subapical actin layer. Comparison to the structural defects caused by inturned depletion revealed striking similarities. Furthermore, coimmunoprecipitation assays demonstrated that the two proteins interact with each other and that Inturned mediates the formation of ternary protein complexes between NPHP4 and DAAM1. Knockdown of daam1, but not formin-2, resulted in similar disruption of the subapical actin web, whereas nphp4 depletion prevented the association of Inturned with the basal bodies. Thus, Inturned appears to function as an adaptor protein that couples cilia-associated molecules to actin-modifying proteins to rearrange the local actin cytoskeleton.

KW - Actin Cytoskeleton

KW - Actins

KW - Adaptor Proteins, Signal Transducing

KW - Animals

KW - Basal Bodies

KW - Cilia

KW - Drosophila melanogaster

KW - Epidermis

KW - Gene Knockdown Techniques

KW - Green Fluorescent Proteins

KW - HEK293 Cells

KW - Humans

KW - Immunoprecipitation

KW - Membrane Proteins

KW - Microfilament Proteins

KW - Molecular Sequence Data

KW - Oligonucleotides

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Proteins

KW - Xenopus Proteins

KW - Xenopus laevis

KW - Journal Article

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

U2 - 10.1083/jcb.201502043

DO - 10.1083/jcb.201502043

M3 - SCORING: Journal article

C2 - 26644512

VL - 211

SP - 963

EP - 973

JO - J CELL BIOL

JF - J CELL BIOL

SN - 0021-9525

IS - 5

ER -