Altered binding of mutated presenilin with cytoskeleton-interacting proteins

Autor:	A A, Johnsingh, J M, Johnston, G, Merz, J, Xu, L, Kotula, J S, Jacobsen, N, Tezapsidis
Rok vydání:	2000
Předmět:	Ionomycin Membrane Proteins Precipitin Tests Neoplasm Proteins Intermediate Filament Proteins Alzheimer Disease Peptide Library Mutation Presenilin-1 Humans Thapsigargin Reed-Sternberg Cells Microtubule-Associated Proteins Conserved Sequence Cytoskeleton
Zdroj:	FEBS letters. 465(1)
ISSN:	0014-5793
Popis:	The majority of familial Alzheimer's disease (AD) cases are linked to mutations on presenilin 1 and 2 genes (PS1 and PS2). The normal function of the proteins and the mechanisms underlying early-onset AD are currently unknown. To address this, we screened an expression library for proteins that bind differentially to the wild-type PS1 and mutant in the large cytoplasmic loop (PS1L). Thus we isolated the C-terminal tail of the 170 kDa cytoplasmic linker protein (CLIP-170) and Reed-Sternberg cells of Hodgkin's disease-expressed intermediate filament-associated protein (Restin), cytoplasmic proteins linking vesicles to the cytoskeleton. PS1L binding to CLIP-170/restin requires Ca(2+). Treating cells with thapsigargin or ionomycin increased the mutated PS1 in CLIP-170 immunoprecipitates. Further, PS1 and CLIP-170 co-localize in transfected cells and neuronal cultures.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::02d57390431f984c3026de63731c8a79 https://pubmed.ncbi.nlm.nih.gov/10620705 Zobrazit plný text záznamu Plný text