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Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation

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Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. / Köttgen, Michael; Benzing, Thomas; Simmen, Thomas; Tauber, Robert; Buchholz, Björn; Feliciangeli, Sylvain; Huber, Tobias B; Schermer, Bernhard; Kramer-Zucker, Albrecht; Höpker, Katja; Simmen, Katia Carmine; Tschucke, Christoph Carl; Sandford, Richard; Kim, Emily; Thomas, Gary; Walz, Gerd.

In: EMBO J, Vol. 24, No. 4, 23.02.2005, p. 705-16.

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

Harvard

Köttgen, M, Benzing, T, Simmen, T, Tauber, R, Buchholz, B, Feliciangeli, S, Huber, TB, Schermer, B, Kramer-Zucker, A, Höpker, K, Simmen, KC, Tschucke, CC, Sandford, R, Kim, E, Thomas, G & Walz, G 2005, 'Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation', EMBO J, vol. 24, no. 4, pp. 705-16. https://doi.org/10.1038/sj.emboj.7600566

APA

Köttgen, M., Benzing, T., Simmen, T., Tauber, R., Buchholz, B., Feliciangeli, S., Huber, T. B., Schermer, B., Kramer-Zucker, A., Höpker, K., Simmen, K. C., Tschucke, C. C., Sandford, R., Kim, E., Thomas, G., & Walz, G. (2005). Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J, 24(4), 705-16. https://doi.org/10.1038/sj.emboj.7600566

Vancouver

Köttgen M, Benzing T, Simmen T, Tauber R, Buchholz B, Feliciangeli S et al. Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J. 2005 Feb 23;24(4):705-16. https://doi.org/10.1038/sj.emboj.7600566

Bibtex

@article{d4c11fd70c1c489096fd0011e4f2c782,
title = "Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation",
abstract = "The trafficking of ion channels to the plasma membrane is tightly controlled to ensure the proper regulation of intracellular ion homeostasis and signal transduction. Mutations of polycystin-2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease, a disorder characterized by renal cysts and progressive renal failure. Polycystin-2 functions as a calcium-permeable nonselective cation channel; however, it is disputed whether polycystin-2 resides and acts at the plasma membrane or endoplasmic reticulum (ER). We show that the subcellular localization and function of polycystin-2 are directed by phosphofurin acidic cluster sorting protein (PACS)-1 and PACS-2, two adaptor proteins that recognize an acidic cluster in the carboxy-terminal domain of polycystin-2. Binding to these adaptor proteins is regulated by the phosphorylation of polycystin-2 by the protein kinase casein kinase 2, required for the routing of polycystin-2 between ER, Golgi and plasma membrane compartments. Our paradigm that polycystin-2 is sorted to and active at both ER and plasma membrane reconciles the previously incongruent views of its localization and function. Furthermore, PACS proteins may represent a novel molecular mechanism for ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments.",
keywords = "Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Carrier Proteins, Cell Line, Endoplasmic Reticulum, Humans, Hydrogen-Ion Concentration, Ion Channels, Membrane Proteins, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein Transport, Sequence Alignment, TRPP Cation Channels, Vesicular Transport Proteins, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.",
author = "Michael K{\"o}ttgen and Thomas Benzing and Thomas Simmen and Robert Tauber and Bj{\"o}rn Buchholz and Sylvain Feliciangeli and Huber, {Tobias B} and Bernhard Schermer and Albrecht Kramer-Zucker and Katja H{\"o}pker and Simmen, {Katia Carmine} and Tschucke, {Christoph Carl} and Richard Sandford and Emily Kim and Gary Thomas and Gerd Walz",
year = "2005",
month = feb,
day = "23",
doi = "10.1038/sj.emboj.7600566",
language = "English",
volume = "24",
pages = "705--16",
journal = "EMBO J",
issn = "0261-4189",
publisher = "NATURE PUBLISHING GROUP",
number = "4",

}

RIS

TY - JOUR

T1 - Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation

AU - Köttgen, Michael

AU - Benzing, Thomas

AU - Simmen, Thomas

AU - Tauber, Robert

AU - Buchholz, Björn

AU - Feliciangeli, Sylvain

AU - Huber, Tobias B

AU - Schermer, Bernhard

AU - Kramer-Zucker, Albrecht

AU - Höpker, Katja

AU - Simmen, Katia Carmine

AU - Tschucke, Christoph Carl

AU - Sandford, Richard

AU - Kim, Emily

AU - Thomas, Gary

AU - Walz, Gerd

PY - 2005/2/23

Y1 - 2005/2/23

N2 - The trafficking of ion channels to the plasma membrane is tightly controlled to ensure the proper regulation of intracellular ion homeostasis and signal transduction. Mutations of polycystin-2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease, a disorder characterized by renal cysts and progressive renal failure. Polycystin-2 functions as a calcium-permeable nonselective cation channel; however, it is disputed whether polycystin-2 resides and acts at the plasma membrane or endoplasmic reticulum (ER). We show that the subcellular localization and function of polycystin-2 are directed by phosphofurin acidic cluster sorting protein (PACS)-1 and PACS-2, two adaptor proteins that recognize an acidic cluster in the carboxy-terminal domain of polycystin-2. Binding to these adaptor proteins is regulated by the phosphorylation of polycystin-2 by the protein kinase casein kinase 2, required for the routing of polycystin-2 between ER, Golgi and plasma membrane compartments. Our paradigm that polycystin-2 is sorted to and active at both ER and plasma membrane reconciles the previously incongruent views of its localization and function. Furthermore, PACS proteins may represent a novel molecular mechanism for ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments.

AB - The trafficking of ion channels to the plasma membrane is tightly controlled to ensure the proper regulation of intracellular ion homeostasis and signal transduction. Mutations of polycystin-2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease, a disorder characterized by renal cysts and progressive renal failure. Polycystin-2 functions as a calcium-permeable nonselective cation channel; however, it is disputed whether polycystin-2 resides and acts at the plasma membrane or endoplasmic reticulum (ER). We show that the subcellular localization and function of polycystin-2 are directed by phosphofurin acidic cluster sorting protein (PACS)-1 and PACS-2, two adaptor proteins that recognize an acidic cluster in the carboxy-terminal domain of polycystin-2. Binding to these adaptor proteins is regulated by the phosphorylation of polycystin-2 by the protein kinase casein kinase 2, required for the routing of polycystin-2 between ER, Golgi and plasma membrane compartments. Our paradigm that polycystin-2 is sorted to and active at both ER and plasma membrane reconciles the previously incongruent views of its localization and function. Furthermore, PACS proteins may represent a novel molecular mechanism for ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments.

KW - Adaptor Proteins, Signal Transducing

KW - Amino Acid Sequence

KW - Carrier Proteins

KW - Cell Line

KW - Endoplasmic Reticulum

KW - Humans

KW - Hydrogen-Ion Concentration

KW - Ion Channels

KW - Membrane Proteins

KW - Molecular Sequence Data

KW - Mutation

KW - Phosphorylation

KW - Protein Binding

KW - Protein Transport

KW - Sequence Alignment

KW - TRPP Cation Channels

KW - Vesicular Transport Proteins

KW - Journal Article

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

KW - Research Support, U.S. Gov't, P.H.S.

U2 - 10.1038/sj.emboj.7600566

DO - 10.1038/sj.emboj.7600566

M3 - SCORING: Journal article

C2 - 15692563

VL - 24

SP - 705

EP - 716

JO - EMBO J

JF - EMBO J

SN - 0261-4189

IS - 4

ER -