The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)

Jennifer Greaves; Gerald R. Prescott; Oforiwa A. Gorleku; Luke H. Chamberlain

doi:10.1080/09687680802620351

The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)

Jennifer Greaves, Gerald R. Prescott, Oforiwa A. Gorleku, Luke H. Chamberlain

School of Biology

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

Abstract

The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes.

Original language	English
Pages (from-to)	67-79
Number of pages	13
Journal	Molecular Membrane Biology
Volume	26
Issue number	1-2
DOIs	https://doi.org/10.1080/09687680802620351
Publication status	Published - 2009

Keywords

Palmitoylation
protein sorting
membrane microdomains
lipid rafts
protein trafficking
CYSTEINE-STRING PROTEIN
GPI-ANCHORED PROTEINS
SRC-FAMILY KINASE
PLASMA-MEMBRANE
LIPID RAFTS
MODEL MEMBRANES
CELL-MEMBRANES
H-RAS
SUBCELLULAR-LOCALIZATION
SACCHAROMYCES-CEREVISIAE

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title = "The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)",

abstract = "The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes.",

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author = "Jennifer Greaves and Prescott, \{Gerald R.\} and Gorleku, \{Oforiwa A.\} and Chamberlain, \{Luke H.\}",

year = "2009",

doi = "10.1080/09687680802620351",

language = "English",

volume = "26",

pages = "67--79",

journal = "Molecular Membrane Biology",

issn = "0968-7688",

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T1 - The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)

AU - Greaves, Jennifer

AU - Prescott, Gerald R.

AU - Gorleku, Oforiwa A.

AU - Chamberlain, Luke H.

PY - 2009

Y1 - 2009

N2 - The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes.

AB - The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes.

KW - Palmitoylation

KW - protein sorting

KW - membrane microdomains

KW - lipid rafts

KW - protein trafficking

KW - CYSTEINE-STRING PROTEIN

KW - GPI-ANCHORED PROTEINS

KW - SRC-FAMILY KINASE

KW - PLASMA-MEMBRANE

KW - LIPID RAFTS

KW - MODEL MEMBRANES

KW - CELL-MEMBRANES

KW - H-RAS

KW - SUBCELLULAR-LOCALIZATION

KW - SACCHAROMYCES-CEREVISIAE

UR - https://www.scopus.com/pages/publications/61449217928

U2 - 10.1080/09687680802620351

DO - 10.1080/09687680802620351

M3 - Review article

SN - 0968-7688

VL - 26

SP - 67

EP - 79

JO - Molecular Membrane Biology

JF - Molecular Membrane Biology

IS - 1-2

ER -

The fat controller: roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review)

Abstract

Keywords

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