Eukaryotic translation initiation factor 2A (eIF2A) is a
protein that in humans is encoded by the EIF2Agene.[5][6][7] The eIF2A protein is not to be confused with
eIF2α, a subunit of the heterotrimeric
eIF2 complex. Instead, eIF2A functions by a separate mechanism in
eukaryotic translation.
Function
eIF2A is a 65 kDa protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes (Zoll et al., 2002).[supplied by OMIM][7] It may be important for translation initiation mediated by the
HCV IRES under stress conditions, but this result has been debated.[8][9]
Wang J, Laschinger C, Zhao XH, Mak B, Seth A, McCulloch CA (Apr 2005). "Mechanical force activates eIF-2alpha phospho-kinases in fibroblast". Biochemical and Biophysical Research Communications. 330 (1): 123–30.
doi:
10.1016/j.bbrc.2005.02.140.
PMID15781241.
Squatrito M, Mancino M, Sala L, Draetta GF (Jun 2006). "Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation". Biochemical and Biophysical Research Communications. 344 (3): 859–68.
doi:
10.1016/j.bbrc.2006.03.205.
PMID16631606.
Eukaryotic translation initiation factor 2A (eIF2A) is a
protein that in humans is encoded by the EIF2Agene.[5][6][7] The eIF2A protein is not to be confused with
eIF2α, a subunit of the heterotrimeric
eIF2 complex. Instead, eIF2A functions by a separate mechanism in
eukaryotic translation.
Function
eIF2A is a 65 kDa protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes (Zoll et al., 2002).[supplied by OMIM][7] It may be important for translation initiation mediated by the
HCV IRES under stress conditions, but this result has been debated.[8][9]
Wang J, Laschinger C, Zhao XH, Mak B, Seth A, McCulloch CA (Apr 2005). "Mechanical force activates eIF-2alpha phospho-kinases in fibroblast". Biochemical and Biophysical Research Communications. 330 (1): 123–30.
doi:
10.1016/j.bbrc.2005.02.140.
PMID15781241.
Squatrito M, Mancino M, Sala L, Draetta GF (Jun 2006). "Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation". Biochemical and Biophysical Research Communications. 344 (3): 859–68.
doi:
10.1016/j.bbrc.2006.03.205.
PMID16631606.