Results: 3

1.
Fig. 2.

Fig. 2. From: 壽Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation.

 TIA-1 and TIAR are related ribonucleic acid (RNA)–binding proteins that possess 3 RNA-recognition motifs and a prion-related domain. Alternative splicing creates 2 isofoms of both proteins

Paul Anderson, et al. Cell Stress Chaperones. 2002 April;7(2):213-221.
2.
Fig. 3.

Fig. 3. From: 壽Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation.

 Regulation of tumor necrosis factor α (TNFα) transcripts by TIA-1. An adenine-uridine–rich element (ARE) tethers TIA-1 to the 3′ untranslated region of TNFα transcripts. This increases the likelihood that TIA-1 will assemble at a noncanonical, translationally silent preinitiation complex, which delivers these transcripts to stress granules (SGs). The SG is proposed to function as a translational checkpoint that monitors mRNP composition and determines whether individual transcripts are stabilized or degraded. The ARE-binding proteins HuR and TTP are proposed to act downstream of the assembly of SGs to influence the functional fate of individual transcripts

Paul Anderson, et al. Cell Stress Chaperones. 2002 April;7(2):213-221.
3.
Fig. 1.

Fig. 1. From: 壽Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation.

 Translational initiation in the absence or presence of stress. (A) Normal: when the eukaryotic translation initiation factor 2 (eIF2)–guanosine triphosphate (GTP)–transfer ribonucleic acid for methionine (tRNAMet) ternary complex is available, a canonical 48S preinitiation complex is assembled at the 5′ end of capped transcripts and scanning begins. Upon recognition of the initiation codon by the anticodon of tRNAMet, eIF5 promotes GTP hydrolysis, and early initiation factors are displaced by the 60S ribosomal subunit. (B) In stressed cells the phosphorylation of eIF2α prevents GDP-GTP exchange by eIF2B, which lowers the effective concentration of eIF2-GTP-tRNAMet. Under these conditions, TIA-1 is included in a noncanonical preinitiation complex that is translationally silent. TIA-1 self-aggregation then promotes the accumulation of these complexes at discrete cytoplasmic foci known as stress granules

Paul Anderson, et al. Cell Stress Chaperones. 2002 April;7(2):213-221.

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk