Applications of proteomic technologies for understanding the premature proteolysis of CFTR

Mark J. Henderson; Om V. Singh; Pamela L. Zeitlin

doi:10.1586/epr.10.42

Applications of proteomic technologies for understanding the premature proteolysis of CFTR

Mark J. Henderson, Om V. Singh, Pamela L. Zeitlin

Research output: Contribution to journal › Review article › peer-review

4 Scopus citations

Abstract

Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene, which encodes an ATP-dependent anion channel. Disease-causing mutations can affect channel biogenesis, trafficking or function, and result in reduced ion transport at the apical surface of many tissues. The most common CFTR mutation is a deletion of phenylalanine at position 508 (F508), which results in a misfolded protein that is prematurely targeted for degradation. This article focuses on how proteomic approaches have been utilized to explore the mechanisms of premature proteolysis in CF. Additionally, we emphasize the potential for proteomic-based technologies in expanding our understanding of CF pathophysiology and therapeutic approaches.

Original language	English (US)
Pages (from-to)	473-486
Number of pages	14
Journal	Expert Review of Proteomics
Volume	7
Issue number	4
DOIs	https://doi.org/10.1586/epr.10.42
State	Published - Aug 2010
Externally published	Yes

Keywords

CFTR
CFTR biogenesis
absolute quantification method
cystic fibrosis
interactomics
proteolysis
proteomics
ubiquitination

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1586/epr.10.42

Cite this

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title = "Applications of proteomic technologies for understanding the premature proteolysis of CFTR",

abstract = "Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene, which encodes an ATP-dependent anion channel. Disease-causing mutations can affect channel biogenesis, trafficking or function, and result in reduced ion transport at the apical surface of many tissues. The most common CFTR mutation is a deletion of phenylalanine at position 508 (F508), which results in a misfolded protein that is prematurely targeted for degradation. This article focuses on how proteomic approaches have been utilized to explore the mechanisms of premature proteolysis in CF. Additionally, we emphasize the potential for proteomic-based technologies in expanding our understanding of CF pathophysiology and therapeutic approaches.",

keywords = "CFTR, CFTR biogenesis, absolute quantification method, cystic fibrosis, interactomics, proteolysis, proteomics, ubiquitination",

author = "Henderson, {Mark J.} and Singh, {Om V.} and Zeitlin, {Pamela L.}",

note = "Funding Information: Support was provided from the National Institutes of Health (R01 HL59410 to Pamela Zeitlin). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.",

year = "2010",

month = aug,

doi = "10.1586/epr.10.42",

language = "English (US)",

volume = "7",

pages = "473--486",

journal = "Expert Review of Proteomics",

issn = "1478-9450",

publisher = "Expert Reviews Ltd.",

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T1 - Applications of proteomic technologies for understanding the premature proteolysis of CFTR

AU - Henderson, Mark J.

AU - Singh, Om V.

AU - Zeitlin, Pamela L.

N1 - Funding Information: Support was provided from the National Institutes of Health (R01 HL59410 to Pamela Zeitlin). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.

PY - 2010/8

Y1 - 2010/8

N2 - Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene, which encodes an ATP-dependent anion channel. Disease-causing mutations can affect channel biogenesis, trafficking or function, and result in reduced ion transport at the apical surface of many tissues. The most common CFTR mutation is a deletion of phenylalanine at position 508 (F508), which results in a misfolded protein that is prematurely targeted for degradation. This article focuses on how proteomic approaches have been utilized to explore the mechanisms of premature proteolysis in CF. Additionally, we emphasize the potential for proteomic-based technologies in expanding our understanding of CF pathophysiology and therapeutic approaches.

AB - Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene, which encodes an ATP-dependent anion channel. Disease-causing mutations can affect channel biogenesis, trafficking or function, and result in reduced ion transport at the apical surface of many tissues. The most common CFTR mutation is a deletion of phenylalanine at position 508 (F508), which results in a misfolded protein that is prematurely targeted for degradation. This article focuses on how proteomic approaches have been utilized to explore the mechanisms of premature proteolysis in CF. Additionally, we emphasize the potential for proteomic-based technologies in expanding our understanding of CF pathophysiology and therapeutic approaches.

KW - CFTR

KW - CFTR biogenesis

KW - absolute quantification method

KW - cystic fibrosis

KW - interactomics

KW - proteolysis

KW - proteomics

KW - ubiquitination

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Applications of proteomic technologies for understanding the premature proteolysis of CFTR

Abstract

Keywords

ASJC Scopus subject areas

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