GSBS Student Publications

Title

Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine

Date

11-30-2005

Document Type

Article

Medical Subject Headings

Amyloid beta-Protein Precursor; Animals; Cell Membrane; Cytoplasm; Gene Library; Mice; Neurons; Phosphorylation; *Polyadenylation; *Protein Biosynthesis; Protein-Serine-Threonine Kinases; RNA, Messenger; RNA-Binding Proteins; Serine; Two-Hybrid System Techniques

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: Mol Cell Biol. 2005 Dec;25(24):10930-9. Link to article on publisher's site

Related Resources

Link to article in PubMed

Journal Title

Molecular and cellular biology

PubMed ID

16314516