An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins

H. M. Burgess; N. K. Gray

doi:10.4161/cib.19347

An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins

H. M. Burgess, N. K. Gray

Deanery of Clinical Sciences

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

Abstract / Description of output

Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.

Original language	English
Pages (from-to)	243-247
Number of pages	5
Journal	Communicative and Integrative Biology
Volume	5
Issue number	3
DOIs	https://doi.org/10.4161/cib.19347
Publication status	Published - May 2012

Keywords / Materials (for Non-textual outputs)

PABP
PABPC1
PABPC4
RNA-binding protein
cellular stress response
nucleo-cytoplasmic transport

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10.4161/cib.19347

An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
Available under Open Acces
Final published version, 2.25 MB

http://www.ncbi.nlm.nih.gov/pubmed/22896784

Poly (A)-binding proteins highlighted the importance of regulated mRNA translation and stability in determing a functional materno-fetal interface
Gray, N., Girardi, G. & Norman, J.
MRC
1/04/12 → 30/09/17
Project: Research

Cite this

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title = "An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins",

abstract = "Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.",

keywords = "PABP, PABPC1, PABPC4, RNA-binding protein, cellular stress response, nucleo-cytoplasmic transport",

author = "Burgess, {H. M.} and Gray, {N. K.}",

note = "Burgess, Hannah M Gray, Nicola K United States Communicative & integrative biology Commun Integr Biol. 2012 May 1;5(3):243-7.",

year = "2012",

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doi = "10.4161/cib.19347",

language = "English",

volume = "5",

pages = "243--247",

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AU - Burgess, H. M.

AU - Gray, N. K.

N1 - Burgess, Hannah M Gray, Nicola K United States Communicative & integrative biology Commun Integr Biol. 2012 May 1;5(3):243-7.

PY - 2012/5

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N2 - Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.

AB - Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.

KW - PABP

KW - PABPC1

KW - PABPC4

KW - RNA-binding protein

KW - cellular stress response

KW - nucleo-cytoplasmic transport

U2 - 10.4161/cib.19347

DO - 10.4161/cib.19347

M3 - Article

C2 - 22896784

VL - 5

SP - 243

EP - 247

JO - Communicative and Integrative Biology

JF - Communicative and Integrative Biology

IS - 3

ER -

An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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Poly (A)-binding proteins highlighted the importance of regulated mRNA translation and stability in determing a functional materno-fetal interface

Cite this