Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation
Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation
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DOI：
10.1128/mcb.25.24.10930-10939.2005
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发表时间：
2005-12-01
影响因子：
5.3
通讯作者：
Richter, JD
中科院分区：
文献类型：
--
作者：
Cao, QP;Huang, YS;Richter, JD
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.
