Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2008 Oct-Dec;2(4):131-4.
doi: 10.4161/pri.2.4.7773. Epub 2008 Oct 3.

Intracellular trafficking and dynamics of P bodies

Affiliations
Review

Intracellular trafficking and dynamics of P bodies

Adva Aizer et al. Prion. 2008 Oct-Dec.

Abstract

RNAs are exported from the nucleus to the cytoplasm, where they undergo translation and produce proteins needed for the cellular life cycle. Some mRNAs are targeted by different RNA decay mechanisms and thereby undergo degradation. The 5'-->3' degradation machinery localizes to cytoplasmic complexes termed P bodies (PBs). They function in RNA turnover, translational repression, RNA-mediated silencing, and RNA storage. A quantitative live-cell imaging approach to study the dynamic aspects of PB trafficking in the cytoplasm revealed that PB movements are rather confined and dependent on an existing microtubule network. Microtubule depolymerization led to a drastic decrease in PB mobility, as well as a release of regulation on PB assembly and a dramatic increase in PB numbers. The different aspects of PB trafficking and encounters with mRNA molecules in the cytoplasm are discussed.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Endogenous PBs were stained with an anti-Dcp1a antibody (red). The nucleus was counterstained with Hoescht (blue) and cells were also imaged in DIC (grey). (A) Normal distribution of PB in human cells. (B) Disruption of the microtubule network using nocodazole (noc) led to an increase in PB numbers. (Bar, 20 µm).

References

    1. Parker R, Song H. The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol. 2004;11:121–127. - PubMed
    1. Bashkirov VI, Scherthan H, Solinger JA, Buerstedde JM, Heyer WD. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J Cell Biol. 1997;136:761–773. - PMC - PubMed
    1. van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, Seraphin B. Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 2002;21:6915–6924. - PMC - PubMed
    1. Ingelfinger D, Arndt-Jovin DJ, Luhrmann R, Achsel T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA. 2002;8:1489–1501. - PMC - PubMed
    1. Lykke-Andersen J. Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol Cell Biol. 2002;22:8114–8121. - PMC - PubMed

Publication types

MeSH terms

LinkOut - more resources