Understanding the rules governing NCX1 palmitoylation

Fiona Plain; Dionne Turnbull; Niall J. Fraser; William Fuller

doi:10.1080/19336950.2017.1342501

Understanding the rules governing NCX1 palmitoylation

Fiona Plain, Dionne Turnbull, Niall J. Fraser, William Fuller (Lead / Corresponding author)

Research output: Contribution to journal › Comment/debate › peer-review

6 Citations (Scopus)

161 Downloads (Pure)

Abstract

The ability to identify sites of post-translational modification in proteins is central to understanding the molecular details of pathways regulating their activity. Through recent advances in mass spectrometry, many of the phosphorylation sites in the human proteome have been experimentally determined, and the kinases responsible predicted according to well-established consensus sequence motifs. However, what of other post-translational modifications? Can we predict these with as much certainty as we can phosphorylation?
Although the palmitoyl proteomes of many different tissues have been determined, reliable palmitoylation site prediction has thus far eluded us.

Original language	English
Pages (from-to)	377-379
Number of pages	3
Journal	Channels
Volume	11
Issue number	5
Early online date	15 Jun 2017
DOIs	https://doi.org/10.1080/19336950.2017.1342501
Publication status	Published - 10 Jul 2017

Keywords

Acylation
Post-translational modification
Sodium
Calcium
Secondary structure
Substrate recognition

Access to Document

10.1080/19336950.2017.1342501

Author Accepted ManuscriptAccepted author manuscript, 758 KB

Palmitoylation of the L-Type Ca Channel Pore-Forming Subunit (joint with University of Bristol)
Fuller, W. (Investigator) & Hales, T. (Investigator)
British Heart Foundation
29/08/16 → 27/02/18
Project: Research
Characterisation of the Cardiac Palmitoyl Transferase DHHC5 (PhD Studentship)
Fraser, N. (Investigator) & Fuller, W. (Investigator)
British Heart Foundation
13/07/15 → 12/07/18
Project: Research
Interaction Between Palmitoylation and Glutathionylation in the Regulation of Cardiac Function
Fuller, W. (Investigator) & Henderson, C. (Investigator)
British Heart Foundation
1/08/13 → 31/07/16
Project: Research

Cite this

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title = "Understanding the rules governing NCX1 palmitoylation",

abstract = "The ability to identify sites of post-translational modification in proteins is central to understanding the molecular details of pathways regulating their activity. Through recent advances in mass spectrometry, many of the phosphorylation sites in the human proteome have been experimentally determined, and the kinases responsible predicted according to well-established consensus sequence motifs. However, what of other post-translational modifications? Can we predict these with as much certainty as we can phosphorylation?Although the palmitoyl proteomes of many different tissues have been determined, reliable palmitoylation site prediction has thus far eluded us.",

keywords = "Acylation , Post-translational modification , Sodium, Calcium, Secondary structure, Substrate recognition",

author = "Fiona Plain and Dionne Turnbull and Fraser, {Niall J.} and William Fuller",

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AU - Plain, Fiona

AU - Turnbull, Dionne

AU - Fraser, Niall J.

AU - Fuller, William

PY - 2017/7/10

Y1 - 2017/7/10

N2 - The ability to identify sites of post-translational modification in proteins is central to understanding the molecular details of pathways regulating their activity. Through recent advances in mass spectrometry, many of the phosphorylation sites in the human proteome have been experimentally determined, and the kinases responsible predicted according to well-established consensus sequence motifs. However, what of other post-translational modifications? Can we predict these with as much certainty as we can phosphorylation?Although the palmitoyl proteomes of many different tissues have been determined, reliable palmitoylation site prediction has thus far eluded us.

AB - The ability to identify sites of post-translational modification in proteins is central to understanding the molecular details of pathways regulating their activity. Through recent advances in mass spectrometry, many of the phosphorylation sites in the human proteome have been experimentally determined, and the kinases responsible predicted according to well-established consensus sequence motifs. However, what of other post-translational modifications? Can we predict these with as much certainty as we can phosphorylation?Although the palmitoyl proteomes of many different tissues have been determined, reliable palmitoylation site prediction has thus far eluded us.

KW - Acylation

KW - Post-translational modification

KW - Sodium

KW - Calcium

KW - Secondary structure

KW - Substrate recognition

U2 - 10.1080/19336950.2017.1342501

DO - 10.1080/19336950.2017.1342501

M3 - Comment/debate

C2 - 28617626

SN - 1933-6950

VL - 11

SP - 377

EP - 379

JO - Channels

JF - Channels

IS - 5

ER -

Understanding the rules governing NCX1 palmitoylation

Abstract

Keywords

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Projects

Palmitoylation of the L-Type Ca Channel Pore-Forming Subunit (joint with University of Bristol)

Characterisation of the Cardiac Palmitoyl Transferase DHHC5 (PhD Studentship)

Interaction Between Palmitoylation and Glutathionylation in the Regulation of Cardiac Function

Cite this