Literature DB >> 2116318

Two phosphorylation sites on eIF-2 alpha.

G Kramer1.   

Abstract

Protein synthesis in mammalian cells can be regulated through phosphorylation/dephosphorylation of the alpha subunit of initiation factor 2, eIF-2. Two specific kinases have been identified that apparently phosphorylate the same site(s). Controversy exists as to whether serine-48 is a phosphorylation site in addition to serine-51. A recent publication is discussed that, in this author's view, answers the question of the phosphorylation sites. It is suggested that phosphorylation proceeds sequentially with serine-51 being the first and serine-48 the second phosphorylation site. Phosphorylation of both sites is required for inhibition of protein synthesis.

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Year:  1990        PMID: 2116318     DOI: 10.1016/0014-5793(90)80919-a

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

Review 1.  Mechanism and regulation of eukaryotic protein synthesis.

Authors:  W C Merrick
Journal:  Microbiol Rev       Date:  1992-06

Review 2.  Regulation of protein turnover in skeletal and cardiac muscle.

Authors:  P H Sugden; S J Fuller
Journal:  Biochem J       Date:  1991-01-01       Impact factor: 3.857

3.  RNA-dependent protein kinase PKR and the Z-DNA binding orthologue PKZ differ in their capacity to mediate initiation factor eIF2α-dependent inhibition of protein synthesis and virus-induced stress granule formation.

Authors:  Nora Taghavi; Charles E Samuel
Journal:  Virology       Date:  2013-05-23       Impact factor: 3.616

4.  Co-activation of Akt, Nrf2, and NF-κB signals under UPRER in torpid Myotis ricketti bats for survival.

Authors:  Wenjie Huang; Chen-Chung Liao; Yijie Han; Junyan Lv; Ming Lei; Yangyang Li; Qingyun Lv; Dong Dong; Shuyi Zhang; Yi-Husan Pan; Jian Luo
Journal:  Commun Biol       Date:  2020-11-11
  4 in total

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