Regulation of SNAP-25 trafficking and function by palmitoylation

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

doi:10.1042/BST0380163

Regulation of SNAP-25 trafficking and function by palmitoylation

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

School of Biology

Research output: Contribution to journal › Article › peer-review

Abstract

The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. in this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein.

Original language	English
Pages (from-to)	163-166
Number of pages	4
Journal	Biochemical Society Transactions
Volume	38
DOIs	https://doi.org/10.1042/BST0380163
Publication status	Published - Feb 2010

Keywords

acylation
aspartate-histidine-histidine-cysteine (DHHC) palmitoyltransferase
exocytosis
palmitoylation
25 kDa synaptosome-associated protein (SNAP-25)
soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE)
CYSTEINE-STRING PROTEIN
HUNTINGTIN-INTERACTING PROTEIN-14
PC12 CELLS
SNARE PROTEINS
LIPID RAFTS
RICH DOMAIN
MEMBRANE LOCALIZATION
SYNAPTIC VESICLES
PLASMA-MEMBRANE
EXOCYTOSIS

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10.1042/BST0380163

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@article{293dd26cfea4480e88fb5161e8564dd9,

title = "Regulation of SNAP-25 trafficking and function by palmitoylation",

abstract = "The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. in this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein.",

keywords = "acylation, aspartate-histidine-histidine-cysteine (DHHC) palmitoyltransferase, exocytosis, palmitoylation, 25 kDa synaptosome-associated protein (SNAP-25), soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE), CYSTEINE-STRING PROTEIN, HUNTINGTIN-INTERACTING PROTEIN-14, PC12 CELLS, SNARE PROTEINS, LIPID RAFTS, RICH DOMAIN, MEMBRANE LOCALIZATION, SYNAPTIC VESICLES, PLASMA-MEMBRANE, EXOCYTOSIS",

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

year = "2010",

month = feb,

doi = "10.1042/BST0380163",

language = "English",

volume = "38",

pages = "163--166",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Regulation of SNAP-25 trafficking and function by palmitoylation

AU - Greaves, Jennifer

AU - Prescott, Gerald R.

AU - Gorleku, Oforiwa A.

AU - Chamberlain, Luke H.

PY - 2010/2

Y1 - 2010/2

N2 - The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. in this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein.

AB - The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. in this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein.

KW - acylation

KW - aspartate-histidine-histidine-cysteine (DHHC) palmitoyltransferase

KW - exocytosis

KW - palmitoylation

KW - 25 kDa synaptosome-associated protein (SNAP-25)

KW - soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE)

KW - CYSTEINE-STRING PROTEIN

KW - HUNTINGTIN-INTERACTING PROTEIN-14

KW - PC12 CELLS

KW - SNARE PROTEINS

KW - LIPID RAFTS

KW - RICH DOMAIN

KW - MEMBRANE LOCALIZATION

KW - SYNAPTIC VESICLES

KW - PLASMA-MEMBRANE

KW - EXOCYTOSIS

U2 - 10.1042/BST0380163

DO - 10.1042/BST0380163

M3 - Article

SN - 0300-5127

VL - 38

SP - 163

EP - 166

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -

Regulation of SNAP-25 trafficking and function by palmitoylation

Abstract

Keywords

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