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Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia

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Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia. / Schermer, Bernhard; Höpker, Katja; Omran, Heymut; Ghenoiu, Cristina; Fliegauf, Manfred; Fekete, Andrea; Horvath, Judit; Köttgen, Michael; Hackl, Matthias; Zschiedrich, Stefan; Huber, Tobias B; Kramer-Zucker, Albrecht; Zentgraf, Hanswalter; Blaukat, Andree; Walz, Gerd; Benzing, Thomas.

in: EMBO J, Jahrgang 24, Nr. 24, 21.12.2005, S. 4415-24.

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

Harvard

Schermer, B, Höpker, K, Omran, H, Ghenoiu, C, Fliegauf, M, Fekete, A, Horvath, J, Köttgen, M, Hackl, M, Zschiedrich, S, Huber, TB, Kramer-Zucker, A, Zentgraf, H, Blaukat, A, Walz, G & Benzing, T 2005, 'Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia', EMBO J, Jg. 24, Nr. 24, S. 4415-24. https://doi.org/10.1038/sj.emboj.7600885

APA

Schermer, B., Höpker, K., Omran, H., Ghenoiu, C., Fliegauf, M., Fekete, A., Horvath, J., Köttgen, M., Hackl, M., Zschiedrich, S., Huber, T. B., Kramer-Zucker, A., Zentgraf, H., Blaukat, A., Walz, G., & Benzing, T. (2005). Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia. EMBO J, 24(24), 4415-24. https://doi.org/10.1038/sj.emboj.7600885

Vancouver

Schermer B, Höpker K, Omran H, Ghenoiu C, Fliegauf M, Fekete A et al. Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia. EMBO J. 2005 Dez 21;24(24):4415-24. https://doi.org/10.1038/sj.emboj.7600885

Bibtex

@article{682f91aaa3e84742995e6159bcdae7f4,
title = "Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia",
abstract = "Mutations in proteins localized to cilia and basal bodies have been implicated in a growing number of human diseases. Access of these proteins to the ciliary compartment requires targeting to the base of the cilia. However, the mechanisms involved in transport of cilia proteins to this transitional zone are elusive. Here we show that nephrocystin, a ciliary protein mutated in the most prevalent form of cystic kidney disease in childhood, is expressed in respiratory epithelial cells and accumulates at the base of cilia, overlapping with markers of the basal body area and the transition zone. Nephrocystin interacts with the phosphofurin acidic cluster sorting protein (PACS)-1. Casein kinase 2 (CK2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates PACS-1 binding, and is essential for colocalization of nephrocystin with PACS-1 at the base of cilia. Inhibition of CK2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting. These data suggest that CK2-dependent transport processes represent a novel pathway of targeting proteins to the cilia.",
keywords = "Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Carrier Proteins, Casein Kinase II, Cell Line, Cell Nucleus, Cilia, Epithelial Cells, Epithelium, Female, Humans, Immunoprecipitation, Membrane Proteins, Mice, Mice, Inbred BALB C, Microscopy, Fluorescence, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Proteins, Serine, Time Factors, Trachea, Transfection, Vesicular Transport Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "Bernhard Schermer and Katja H{\"o}pker and Heymut Omran and Cristina Ghenoiu and Manfred Fliegauf and Andrea Fekete and Judit Horvath and Michael K{\"o}ttgen and Matthias Hackl and Stefan Zschiedrich and Huber, {Tobias B} and Albrecht Kramer-Zucker and Hanswalter Zentgraf and Andree Blaukat and Gerd Walz and Thomas Benzing",
year = "2005",
month = dec,
day = "21",
doi = "10.1038/sj.emboj.7600885",
language = "English",
volume = "24",
pages = "4415--24",
journal = "EMBO J",
issn = "0261-4189",
publisher = "NATURE PUBLISHING GROUP",
number = "24",

}

RIS

TY - JOUR

T1 - Phosphorylation by casein kinase 2 induces PACS-1 binding of nephrocystin and targeting to cilia

AU - Schermer, Bernhard

AU - Höpker, Katja

AU - Omran, Heymut

AU - Ghenoiu, Cristina

AU - Fliegauf, Manfred

AU - Fekete, Andrea

AU - Horvath, Judit

AU - Köttgen, Michael

AU - Hackl, Matthias

AU - Zschiedrich, Stefan

AU - Huber, Tobias B

AU - Kramer-Zucker, Albrecht

AU - Zentgraf, Hanswalter

AU - Blaukat, Andree

AU - Walz, Gerd

AU - Benzing, Thomas

PY - 2005/12/21

Y1 - 2005/12/21

N2 - Mutations in proteins localized to cilia and basal bodies have been implicated in a growing number of human diseases. Access of these proteins to the ciliary compartment requires targeting to the base of the cilia. However, the mechanisms involved in transport of cilia proteins to this transitional zone are elusive. Here we show that nephrocystin, a ciliary protein mutated in the most prevalent form of cystic kidney disease in childhood, is expressed in respiratory epithelial cells and accumulates at the base of cilia, overlapping with markers of the basal body area and the transition zone. Nephrocystin interacts with the phosphofurin acidic cluster sorting protein (PACS)-1. Casein kinase 2 (CK2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates PACS-1 binding, and is essential for colocalization of nephrocystin with PACS-1 at the base of cilia. Inhibition of CK2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting. These data suggest that CK2-dependent transport processes represent a novel pathway of targeting proteins to the cilia.

AB - Mutations in proteins localized to cilia and basal bodies have been implicated in a growing number of human diseases. Access of these proteins to the ciliary compartment requires targeting to the base of the cilia. However, the mechanisms involved in transport of cilia proteins to this transitional zone are elusive. Here we show that nephrocystin, a ciliary protein mutated in the most prevalent form of cystic kidney disease in childhood, is expressed in respiratory epithelial cells and accumulates at the base of cilia, overlapping with markers of the basal body area and the transition zone. Nephrocystin interacts with the phosphofurin acidic cluster sorting protein (PACS)-1. Casein kinase 2 (CK2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates PACS-1 binding, and is essential for colocalization of nephrocystin with PACS-1 at the base of cilia. Inhibition of CK2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting. These data suggest that CK2-dependent transport processes represent a novel pathway of targeting proteins to the cilia.

KW - Adaptor Proteins, Signal Transducing

KW - Amino Acid Sequence

KW - Animals

KW - Antibodies, Monoclonal

KW - Carrier Proteins

KW - Casein Kinase II

KW - Cell Line

KW - Cell Nucleus

KW - Cilia

KW - Epithelial Cells

KW - Epithelium

KW - Female

KW - Humans

KW - Immunoprecipitation

KW - Membrane Proteins

KW - Mice

KW - Mice, Inbred BALB C

KW - Microscopy, Fluorescence

KW - Molecular Sequence Data

KW - Phosphorylation

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Proteins

KW - Serine

KW - Time Factors

KW - Trachea

KW - Transfection

KW - Vesicular Transport Proteins

KW - Journal Article

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

U2 - 10.1038/sj.emboj.7600885

DO - 10.1038/sj.emboj.7600885

M3 - SCORING: Journal article

C2 - 16308564

VL - 24

SP - 4415

EP - 4424

JO - EMBO J

JF - EMBO J

SN - 0261-4189

IS - 24

ER -