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Eif2ak3  -  eukaryotic translation initiation factor 2...

Mus musculus

Synonyms: AI427929, Eukaryotic translation initiation factor 2-alpha kinase 3, PERK, PRKR-like endoplasmic reticulum kinase, Pancreatic eIF2-alpha kinase, ...
 
 
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Disease relevance of Eif2ak3

 

High impact information on Eif2ak3

  • The exocrine and endocrine pancreas developed normally in Perk-/- mice [3].
  • Here, we show that tumors derived from K-Ras-transformed Perk(-/-) mouse embryonic fibroblasts (MEFs) are smaller and exhibit less angiogenesis than tumors with an intact ISR [4].
  • This analysis revealed that a subset of proangiogenic transcripts is preferentially translated in a Perk-dependent manner; these transcripts include VCIP, an adhesion molecule that promotes cellular adhesion, integrin binding, and capillary morphogenesis [4].
  • Endoplasmic reticulum (ER) stress is not effectively induced in MEF cells subjected to proteasome inhibition, with minimal activation of the ER stress sensory proteins, eIF2alpha kinase PEK (PERK/EIF2AK3), IRE1 protein kinase and the transcription regulator ATF6 following up to 6 h of proteasome inhibitor treatment [5].
  • Injections of IGF-I partially reversed the growth retardation of the Perk-/- mice, whereas GH had no effect [1].
 

Anatomical context of Eif2ak3

  • Overexpression of ATF3 in mouse embryo fibroblasts partially bypasses the requirement for PEK for induction of GADD34 in response to ER stress, further supporting the idea that ATF3 functions directly or indirectly as a transcriptional activator of genes targeted by the eIF2 kinase stress pathway [6].
 

Other interactions of Eif2ak3

  • However, the recent identification of a trans-microsomal membrane eIF2alpha kinase, termed PEK or PERK, suggests that this kinase, and not PKR, might be the kinase that is activated by misfolded protein accumulation [7].
 

Analytical, diagnostic and therapeutic context of Eif2ak3

  • These observations were corroborated by a microarray analysis of polysome-bound RNA in aerobic and hypoxic Perk(+/+) and Perk(-/-) MEFs [4].

References

  1. PERK eIF2alpha kinase regulates neonatal growth by controlling the expression of circulating insulin-like growth factor-I derived from the liver. Li, Y., Iida, K., O'Neil, J., Zhang, P., Li, S., Frank, A., Gabai, A., Zambito, F., Liang, S.H., Rosen, C.J., Cavener, D.R. Endocrinology (2003) [Pubmed]
  2. PERK is responsible for the increased phosphorylation of eIF2alpha and the severe inhibition of protein synthesis after transient global brain ischemia. Owen, C.R., Kumar, R., Zhang, P., McGrath, B.C., Cavener, D.R., Krause, G.S. J. Neurochem. (2005) [Pubmed]
  3. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Harding, H.P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D.D., Ron, D. Mol. Cell (2001) [Pubmed]
  4. Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress. Blais, J.D., Addison, C.L., Edge, R., Falls, T., Zhao, H., Wary, K., Koumenis, C., Harding, H.P., Ron, D., Holcik, M., Bell, J.C. Mol. Cell. Biol. (2006) [Pubmed]
  5. Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. Jiang, H.Y., Wek, R.C. J. Biol. Chem. (2005) [Pubmed]
  6. Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response. Jiang, H.Y., Wek, S.A., McGrath, B.C., Lu, D., Hai, T., Harding, H.P., Wang, X., Ron, D., Cavener, D.R., Wek, R.C. Mol. Cell. Biol. (2004) [Pubmed]
  7. The double-stranded RNA-activated protein kinase PKR is dispensable for regulation of translation initiation in response to either calcium mobilization from the endoplasmic reticulum or essential amino acid starvation. Kimball, S.R., Clemens, M.J., Tilleray, V.J., Wek, R.C., Horetsky, R.L., Jefferson, L.S. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
 
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