Translational control from head to tail

Groppo, Rachel; Richter, Joel D.

doi:10.1016/j.ceb.2009.01.011

Cited by 51 publications

(48 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…106,107 Broad translational control mechanisms that likely act upon most mRNAs include phosphorylation of the initiation factor eIF2a by various stress-responsive kinases, 109 which limits levels of ternary complex, and thus, translation initiation rates. This event facilitates assembly of stress granules under most (but not all) circumstances.…”

Section: Role Of Mrnp Granules In Translational Controlmentioning

confidence: 99%

mRNP granules

2014

View full text Add to dashboard Cite

Section: Role Of Mrnp Granules In Translational Controlmentioning

confidence: 99%

mRNP granules

2014

View full text Add to dashboard Cite

“…Not all homologs of eIF4E have a role in constitutive translation initiation (Rhoads 2009); they may function as competitive inhibitors of eIF4G recruitment and as scaffolds for interactions with other potential regulatory proteins (Groppo and Richter 2009;Blewett and Goldstrohm 2012;Gosselin et al 2013). Some eIF4E-binding proteins like 4E-BP repress translation by inhibiting eIF4F formation, whereas other eIF4E-binding proteins, such as Cup and Maskin, use alternative 3 ′ UTRprotein interactions for selective repression of translation (Groppo and Richter 2009). Further, selective translation of mRNAs can occur via cap binding of an eIF4E homologous protein, 4E-HP ) and discrete protein-3 ′ UTR interactions .…”

Section: Introductionmentioning

confidence: 99%

eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

Freire

Vashisht

Malvezzi

et al. 2014

RNA

View full text Add to dashboard Cite

Members of the eIF4E mRNA cap-binding family are involved in translation and the modulation of transcript availability in other systems as part of a three-component complex including eIF4G and eIF4A. The kinetoplastids possess four described eIF4E and five eIF4G homologs. We have identified two new eIF4E family proteins in Trypanosoma brucei, and define distinct complexes associated with the fifth member, TbEIF4E5. The cytosolic TbEIF4E5 protein binds cap 0 in vitro. TbEIF4E5 was found in association with two of the five TbEIF4Gs. TbIF4EG1 bound TbEIF4E5, a 47.5-kDa protein with two RNA-binding domains, and either the regulatory protein 14-3-3 II or a 117.5-kDa protein with guanylyltransferase and methyltransferase domains in a potentially dynamic interaction. The TbEIF4G2/TbEIF4E5 complex was associated with a 17.9-kDa hypothetical protein and both 14-3-3 variants I and II. Knockdown of TbEIF4E5 resulted in the loss of productive cell movement, as evidenced by the inability of the cells to remain in suspension in liquid culture and the loss of social motility on semisolid plating medium, as well as a minor reduction of translation. Cells appeared lethargic, as opposed to compromised in flagellar function per se. The minimal use of transcriptional control in kinetoplastids requires these organisms to implement downstream mechanisms to regulate gene expression, and the TbEIF4E5/TbEIF4G1/117.5-kDa complex in particular may be a key player in that process. We suggest that a pathway involved in cell motility is affected, directly or indirectly, by one of the TbEIF4E5 complexes.

show abstract

“…1,2 The RNA binding protein, Fragile-X-Mental-Retardation-syndrome-Related protein 1 (FXR1) [3][4][5] is overexpressed and associated with poor clinical outcomes in multiple cancers. 6 FXR1 is similar to Fragile-X-Mental Retardation Protein 1 (FMR1), 4,[7][8][9][10][11][12][13][14] and is implicated at multiple levels of post-transcriptional control, including translation, mRNA stability and transport.…”

Section: Introductionmentioning

confidence: 99%

Regulation of monocyte induced cell migration by the RNA binding protein, FXR1

et al. 2016

View full text Add to dashboard Cite

FXR1 belongs to a family of RNA-binding proteins that play critical roles in post-transcriptional regulation of gene expression in immunity, development and cancer. FXR1 is associated with regulation of specific mRNAs in myocytes and macrophages. In quiescent cells (> 24 h of extended serum-starvation, »30-48 h or more), a spliced isoform of FXR1, FXR1a, promotes translation of the cytokine TNFa, independent of the effects of RNA levels. Here we examined the role of FXR1 in THP1 human monocytic leukemic cells that were grown in serum, as well as in early (24 h) serum-starvation conditions that demonstrates differences in gene expression mechanisms and is distinct from quiescent (> 24 h extended serum-starvation) cells. Global RNA profiling, conducted to investigate the role of FXR1 on mRNA levels, revealed that FXR1 affects levels of specific mRNAs in serum-grown and in early 24 h serum-starvation conditions. FXR1 decreases levels of several mRNAs, including as previously identified, CDKN1A (p21CIP1 or p21) mRNA in serumgrown cells. Interestingly, we find that FXR1 positively regulates mRNA levels of specific cytokines and chemokines in serum-grown and in early 24 h serum-starvation conditions. These include IL1b and CCL2 that control cell migration. Accordingly, depletion and overexpression of FXR1 decreased and increased levels of CCL2 mRNA. Consistent with the reduced levels of IL1b, CCL2 and other chemokines upon FXR1 depletion, our data reveal that depletion of FXR1 decreases the ability of these cells to induce cell migration of neighboring monocytic cells. These data reveal a new role of FXR1 in controlling induction of monocyte migration.

show abstract

Translational control from head to tail

Cited by 51 publications

References 58 publications

mRNP granules

mRNP granules

eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

Regulation of monocyte induced cell migration by the RNA binding protein, FXR1

Contact Info

Product

Resources

About