Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage.

The Journal of biological chemistry - 20 Dec 2002

Kim Doo Yeon, Ingano Laura A MacKenzie, Kovacs Dora M

Abstract excerpt

Nectin-1 is a member of the immunoglobulin superfamily and a Ca(2+)-independent adherens junction protein involved in synapse formation. Here we show that nectin-1alpha undergoes intramembrane proteolytic processing analogous to that of the Alzheimer's disease amyloid precursor protein, mediated by a presenilin (PS)-dependent gamma-secretase-like activity. 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adherens Junctions
Share to Amyloid Precursor Protein Secretases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Aspartic Acid Endopeptidases

Share to Cysteine Endopeptidases

Share to Endopeptidases

Share to Multienzyme Complexes

Share to Nectins

Share to Presenilin-1

Source

Identifiers

PMID: 12376527
DOI: 10.1074/jbc.M210179200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage.PMID 12376527Read ↗

Characterization of sequential N-cadherin cleavage by ADAM10 and PS1.Semantic proximity Read ↗

Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.Semantic proximity Read ↗

Tumor necrosis factor-alpha-elicited stimulation of gamma-secretase is mediated by c-Jun N-terminal kinase-dependent phosphorylation of presenilin and nicastrin.Semantic proximity Read ↗

The presenilin proteins are components of multiple membrane-bound complexes that have different biological activities.Semantic proximity Read ↗

Nectin family of cell-adhesion molecules: structural and molecular aspects of function and specificitySemantic proximity Read ↗

Different cofactor activities in gamma-secretase assembly: evidence for a nicastrin-Aph-1 subcomplex.Semantic proximity Read ↗

Nectin and Nectin-Like Molecules: Biology and PathologySemantic proximity Read ↗

Novel processing of Notch 1 within its intracellular domain by a cysteine protease.Semantic proximity Read ↗

Caspase cleaved presenilin-1 is part of active gamma-secretase complexes.Semantic proximity Read ↗

Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.Semantic proximity Read ↗

Presenilin-1: a component of synaptic and endothelial adherens junctions.Semantic proximity Read ↗

Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.