| First Author | Cao Q | Year | 2005 |
| Journal | Mol Cell Biol | Volume | 25 |
| Issue | 24 | Pages | 10930-9 |
| PubMed ID | 16314516 | Mgi Jnum | J:103763 |
| Mgi Id | MGI:3610697 | Doi | 10.1128/MCB.25.24.10930-10939.2005 |
| Citation | Cao Q, et al. (2005) Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation. Mol Cell Biol 25(24):10930-9 |
| abstractText | The cytoplasmic polyadenylation element (CPE) binding factor, CPEB, is a sequence-specific RNA binding protein that controls polyadenylation-induced translation in germ cells and at postsynaptic sites of neurons. A yeast two-hybrid screen with a mouse brain cDNA library identified the transmembrane amyloid precursor-like protein 1 (APLP1) as a CPEB-interacting factor. CPEB binds the small intracellular domain (ICD) of APLP1 and the related proteins APLP2 and APP. These proteins promote polyadenylation and translation by stimulating Aurora A catalyzed CPEB serine 174 phosphorylation. Surprisingly, CPEB, Maskin, CPSF, and several other factors involved in polyadenylation and translation and CPE-containing RNA are all detected on membranes by cell fractionation and immunoelectron microscopy. Moreover, most of the RNA that undergoes polyadenylation does so in membrane-containing fractions. These data demonstrate a link between cytoplasmic polyadenylation and membrane association and implicate APP family member proteins as anchors for localized mRNA polyadenylation and translation. |
