Detection of heterogeneous protein S-acylation in cells

Jennifer Greaves; Nicholas C. O. Tomkinson

doi:10.1007/978-1-4939-9532-5_2

Detection of heterogeneous protein S-acylation in cells

Jennifer Greaves, Nicholas C. O. Tomkinson

Pure And Applied Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Entry for encyclopedia/dictionary

14 Downloads (Pure)

Abstract

The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(i)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.

Original language	English
Title of host publication	Protein Lipidation
Subtitle of host publication	Methods and Protocols
Editors	Maurine E. Linder
Place of Publication	New York
Publisher	Springer
Pages	13-33
Number of pages	21
ISBN (Electronic)	978-1-4939-9532-5
ISBN (Print)	978-1-4939-9531-8
DOIs	https://doi.org/10.1007/978-1-4939-9532-5_2
Publication status	Published - 1 Jun 2019

Keywords

click chemistry
fatty acid azide
fatty acylation
palmitoylation
s-acylation

Access to Document

10.1007/978-1-4939-9532-5_2

Greaves-Tomkinson-Springer-2019-Detection-of-heterogeneous-protein-S-acylation-inAccepted author manuscript, 207 KB

Cite this

@inbook{7882d93dda244288bb0f15d6cb6576fc,

title = "Detection of heterogeneous protein S-acylation in cells",

abstract = "The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(i)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.",

keywords = "click chemistry, fatty acid azide, fatty acylation, palmitoylation, s-acylation",

author = "Jennifer Greaves and Tomkinson, {Nicholas C. O.}",

year = "2019",

month = jun,

day = "1",

doi = "10.1007/978-1-4939-9532-5_2",

language = "English",

isbn = "978-1-4939-9531-8",

pages = "13--33",

editor = "Linder, {Maurine E.}",

booktitle = "Protein Lipidation",

publisher = "Springer",

}

TY - CHAP

T1 - Detection of heterogeneous protein S-acylation in cells

AU - Greaves, Jennifer

AU - Tomkinson, Nicholas C. O.

PY - 2019/6/1

Y1 - 2019/6/1

N2 - The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(i)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.

AB - The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(i)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.

KW - click chemistry

KW - fatty acid azide

KW - fatty acylation

KW - palmitoylation

KW - s-acylation

U2 - 10.1007/978-1-4939-9532-5_2

DO - 10.1007/978-1-4939-9532-5_2

M3 - Entry for encyclopedia/dictionary

SN - 978-1-4939-9531-8

SP - 13

EP - 33

BT - Protein Lipidation

A2 - Linder, Maurine E.

PB - Springer

CY - New York

ER -

Detection of heterogeneous protein S-acylation in cells

Abstract

Keywords

Access to Document

Fingerprint

Cite this