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PMID: 8855266 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 20 ·1996-10-01 ·Pages 10832-7

Guénette SY, Chen J, Jondro PD, Tanzi RE

Abstract

We identified a novel human homologue of the rat FE65 gene, hFE65L, by screening the cytoplasmic domain of beta-amyloid precursor protein (beta PP) with the "interaction trap." The cytoplasmic domains of the beta PP homologues, APLP1 and APLP2 (amyloid precursor-like proteins), were also tested for interaction with hFE65L. APLP2, but not APLP1, was found to interact with hFE65L. We confirmed these interactions in vivo by successfully coimmunoprecipatating endogenous beta PP and APLP2 from mammalian cells overexpressing a hemagglutinin-tagged fusion of the C-terminal region of hFE65L. We report the existence of a human FE65 gene family and evidence supporting specific interactions between members of the beta PP and FE65 protein families. Sequence analysis of the FE65 human gene family reveals the presence of two phosphotyrosine interaction (PI) domains. Our data show that a single PI domain is sufficient for binding of hFE65L to the cytoplasmic domain of beta PP and APLP2. The PI domain of the protein, Shc, is known to interact with the NPXYp motif found in the cytoplasmic domain of a number of different growth factor receptors. Thus, it is likely that the PI domains present in the C-terminal moiety of the hFE65L protein bind the NPXY motif located in the cytoplasmic domain of beta PP and APLP2.

MeSH Terms
Amino Acid Sequence Amyloid beta-Protein Precursor/metabolism Animals Cloning, Molecular Cytoplasm Gene Expression Humans Molecular Sequence Data Multigene Family Nerve Tissue Proteins/genetics,metabolism Nuclear Proteins/genetics,metabolism Precipitin Tests Protein Binding Rats Recombinant Proteins/metabolism Sequence Alignment Sequence Homology, Amino Acid
Chemicals
APBB1 protein, human Amyloid beta-Protein Precursor Apbb1 protein, rat Nerve Tissue Proteins Nuclear Proteins Recombinant Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Guénette S Y
Genetics and Aging Unit, Massachusetts General Hospital-East, Harvard Medical School, Charlestown 02129, USA.
Chen J
Jondro P D
Tanzi R E
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.20.10832
Published
1996-10-01
Pages
10832-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC38241
Subset
IM
Databases
GENBANK
D56274, F07610, R67159, R84592, R87225, T09348, T31017, T54909, U62325
External Links
PubMed source DOI: 10.1073/pnas.93.20.10832 PMC Full Text View journal details
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