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

Deanery of Biomedical Sciences

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

Abstract / Description of output

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

Access to Document

10.1042/BST0380163

Cite this

@article{e6a1eb3fc1e84a41bd190ff5f2a77728,

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.",

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.

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 / Description of output

Access to Document

Fingerprint

Cite this