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The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins

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The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins. / Höhne, Martin; Lorscheider, Johannes; von Bardeleben, Anna; Dufner, Matthias; Scharf, M Antonia; Gödel, Markus; Helmstädter, Martin; Schurek, Eva-Maria; Zank, Sibylle; Gerke, Peter; Kurschat, Christine; Sivritas, Sema Hayriye; Neumann-Haefelin, Elke; Huber, Tobias B; Reinhardt, H Christian; Schauss, Astrid C; Schermer, Bernhard; Fischbach, Karl-Friedrich; Benzing, Thomas.

in: MOL CELL BIOL, Jahrgang 31, Nr. 16, 08.2011, S. 3241-51.

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

Harvard

Höhne, M, Lorscheider, J, von Bardeleben, A, Dufner, M, Scharf, MA, Gödel, M, Helmstädter, M, Schurek, E-M, Zank, S, Gerke, P, Kurschat, C, Sivritas, SH, Neumann-Haefelin, E, Huber, TB, Reinhardt, HC, Schauss, AC, Schermer, B, Fischbach, K-F & Benzing, T 2011, 'The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins', MOL CELL BIOL, Jg. 31, Nr. 16, S. 3241-51. https://doi.org/10.1128/MCB.05286-11

APA

Höhne, M., Lorscheider, J., von Bardeleben, A., Dufner, M., Scharf, M. A., Gödel, M., Helmstädter, M., Schurek, E-M., Zank, S., Gerke, P., Kurschat, C., Sivritas, S. H., Neumann-Haefelin, E., Huber, T. B., Reinhardt, H. C., Schauss, A. C., Schermer, B., Fischbach, K-F., & Benzing, T. (2011). The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins. MOL CELL BIOL, 31(16), 3241-51. https://doi.org/10.1128/MCB.05286-11

Vancouver

Höhne M, Lorscheider J, von Bardeleben A, Dufner M, Scharf MA, Gödel M et al. The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins. MOL CELL BIOL. 2011 Aug;31(16):3241-51. https://doi.org/10.1128/MCB.05286-11

Bibtex

@article{5d743d456fdf44f5a2c4f6d0d8e5e785,
title = "The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins",
abstract = "Neph proteins are evolutionarily conserved membrane proteins of the immunoglobulin superfamily that control the formation of specific intercellular contacts. Cell recognition through these proteins is essential in diverse cellular contexts such as patterning of the compound eye in Drosophila melanogaster, neuronal connectivity in Caenorhabditis elegans, and the formation of the kidney filtration barrier in mammals. Here we identify the PDZ and BAR domain protein PICK1 (protein interacting with C-kinase 1) as a Neph-interacting protein. Binding required dimerization of PICK1, was dependent on PDZ domain protein interactions, and mediated stabilization of Neph1 at the plasma membrane. Moreover, protein kinase C (PKCα) activity facilitated the interaction through releasing Neph proteins from their binding to the multidomain scaffolding protein zonula occludens 1 (ZO-1), another PDZ domain protein. In Drosophila, the Neph homologue Roughest is essential for sorting of interommatidial precursor cells and patterning of the compound eye. RNA interference-mediated knockdown of PICK1 in the Drosophila eye imaginal disc caused a Roughest destabilization at the plasma membrane and a phenotype that resembled rst mutation. These data indicate that Neph proteins and PICK1 synergistically regulate cell recognition and contact formation.",
keywords = "Animals, Carrier Proteins, Cell Communication, Drosophila, Drosophila melanogaster, Eye, Humans, Membrane Proteins, Morphogenesis, Nuclear Proteins, PDZ Domains, Protein Binding, Protein Kinase C, Protein Multimerization, Protein Stability, Protein Structure, Tertiary, Journal Article, Research Support, Non-U.S. Gov't",
author = "Martin H{\"o}hne and Johannes Lorscheider and {von Bardeleben}, Anna and Matthias Dufner and Scharf, {M Antonia} and Markus G{\"o}del and Martin Helmst{\"a}dter and Eva-Maria Schurek and Sibylle Zank and Peter Gerke and Christine Kurschat and Sivritas, {Sema Hayriye} and Elke Neumann-Haefelin and Huber, {Tobias B} and Reinhardt, {H Christian} and Schauss, {Astrid C} and Bernhard Schermer and Karl-Friedrich Fischbach and Thomas Benzing",
year = "2011",
month = aug,
doi = "10.1128/MCB.05286-11",
language = "English",
volume = "31",
pages = "3241--51",
journal = "MOL CELL BIOL",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "16",

}

RIS

TY - JOUR

T1 - The BAR domain protein PICK1 regulates cell recognition and morphogenesis by interacting with Neph proteins

AU - Höhne, Martin

AU - Lorscheider, Johannes

AU - von Bardeleben, Anna

AU - Dufner, Matthias

AU - Scharf, M Antonia

AU - Gödel, Markus

AU - Helmstädter, Martin

AU - Schurek, Eva-Maria

AU - Zank, Sibylle

AU - Gerke, Peter

AU - Kurschat, Christine

AU - Sivritas, Sema Hayriye

AU - Neumann-Haefelin, Elke

AU - Huber, Tobias B

AU - Reinhardt, H Christian

AU - Schauss, Astrid C

AU - Schermer, Bernhard

AU - Fischbach, Karl-Friedrich

AU - Benzing, Thomas

PY - 2011/8

Y1 - 2011/8

N2 - Neph proteins are evolutionarily conserved membrane proteins of the immunoglobulin superfamily that control the formation of specific intercellular contacts. Cell recognition through these proteins is essential in diverse cellular contexts such as patterning of the compound eye in Drosophila melanogaster, neuronal connectivity in Caenorhabditis elegans, and the formation of the kidney filtration barrier in mammals. Here we identify the PDZ and BAR domain protein PICK1 (protein interacting with C-kinase 1) as a Neph-interacting protein. Binding required dimerization of PICK1, was dependent on PDZ domain protein interactions, and mediated stabilization of Neph1 at the plasma membrane. Moreover, protein kinase C (PKCα) activity facilitated the interaction through releasing Neph proteins from their binding to the multidomain scaffolding protein zonula occludens 1 (ZO-1), another PDZ domain protein. In Drosophila, the Neph homologue Roughest is essential for sorting of interommatidial precursor cells and patterning of the compound eye. RNA interference-mediated knockdown of PICK1 in the Drosophila eye imaginal disc caused a Roughest destabilization at the plasma membrane and a phenotype that resembled rst mutation. These data indicate that Neph proteins and PICK1 synergistically regulate cell recognition and contact formation.

AB - Neph proteins are evolutionarily conserved membrane proteins of the immunoglobulin superfamily that control the formation of specific intercellular contacts. Cell recognition through these proteins is essential in diverse cellular contexts such as patterning of the compound eye in Drosophila melanogaster, neuronal connectivity in Caenorhabditis elegans, and the formation of the kidney filtration barrier in mammals. Here we identify the PDZ and BAR domain protein PICK1 (protein interacting with C-kinase 1) as a Neph-interacting protein. Binding required dimerization of PICK1, was dependent on PDZ domain protein interactions, and mediated stabilization of Neph1 at the plasma membrane. Moreover, protein kinase C (PKCα) activity facilitated the interaction through releasing Neph proteins from their binding to the multidomain scaffolding protein zonula occludens 1 (ZO-1), another PDZ domain protein. In Drosophila, the Neph homologue Roughest is essential for sorting of interommatidial precursor cells and patterning of the compound eye. RNA interference-mediated knockdown of PICK1 in the Drosophila eye imaginal disc caused a Roughest destabilization at the plasma membrane and a phenotype that resembled rst mutation. These data indicate that Neph proteins and PICK1 synergistically regulate cell recognition and contact formation.

KW - Animals

KW - Carrier Proteins

KW - Cell Communication

KW - Drosophila

KW - Drosophila melanogaster

KW - Eye

KW - Humans

KW - Membrane Proteins

KW - Morphogenesis

KW - Nuclear Proteins

KW - PDZ Domains

KW - Protein Binding

KW - Protein Kinase C

KW - Protein Multimerization

KW - Protein Stability

KW - Protein Structure, Tertiary

KW - Journal Article

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

U2 - 10.1128/MCB.05286-11

DO - 10.1128/MCB.05286-11

M3 - SCORING: Journal article

C2 - 21690291

VL - 31

SP - 3241

EP - 3251

JO - MOL CELL BIOL

JF - MOL CELL BIOL

SN - 0270-7306

IS - 16

ER -