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

University of Edinburgh

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

18 Citations (Scopus)

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
Issue number	Pt 1
DOIs	https://doi.org/10.1042/BST0380163
Publication status	Published - Feb 2010
Externally published	Yes

Keywords

Acyltransferases
Animals
Exocytosis
Humans
Lipoylation
Protein Transport
Synaptosomal-Associated Protein 25
Journal Article
Research Support, Non-U.S. Gov't
Review

Access to Document

10.1042/BST0380163

Cite this

@article{ee2519ff31b34b4aacd88d5051998e60,

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 = "Acyltransferases, Animals, Exocytosis, Humans, Lipoylation, Protein Transport, Synaptosomal-Associated Protein 25, Journal Article, Research Support, Non-U.S. Gov't, Review",

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",

number = "Pt 1",

}

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 - Acyltransferases

KW - Animals

KW - Exocytosis

KW - Humans

KW - Lipoylation

KW - Protein Transport

KW - Synaptosomal-Associated Protein 25

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1042/BST0380163

DO - 10.1042/BST0380163

M3 - Review article

C2 - 20074052

SN - 0300-5127

VL - 38

SP - 163

EP - 166

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

IS - Pt 1

ER -

Regulation of SNAP-25 trafficking and function by palmitoylation

Abstract

Keywords

Access to Document

Fingerprint

Cite this