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Erythrocyte membrane protein band 4.1-like 1

4.1N, EPB41L1
Erythrocyte membrane protein band 4.1 (EPB41) is a multifunctional protein that mediates interactions between the erythrocyte cytoskeleton and the overlying plasma membrane. The protein encoded by this gene is a neuronally-enriched protein that is structurally similar to EPB41. The encoded protein binds and stabilizes D2 and D3 dopamine receptors at the neuronal plasma membrane. Multiple transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them has been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: 4.1B, 4.1 g, Actin, V1a, HAD
Papers on 4.1N
A Critical Role for the GluA1 Accessory Protein, SAP97, in Cocaine Seeking.
Pierce et al., Philadelphia, United States. In Neuropsychopharmacology, Feb 2016
SAP97 and 4.1N are proteins involved in GluA1 trafficking to and stabilization in synapses; SAP97-GluA1 interactions also influence dendritic growth.
4.1N suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer cells.
Liu et al., Beijing, China. In Mol Med Report, Jan 2016
Protein 4.1N (4.1N) is a member of the protein 4.1 family and is essential for the regulation of cell adhesion, motility and signaling.
Protein 4.1N acts as a potential tumor suppressor linking PP1 to JNK-c-Jun pathway regulation in NSCLC.
Liu et al., Changsha, China. In Oncotarget, Dec 2015
UNASSIGNED: Protein 4.1N is a member of protein 4.1 family and has been recognized as a potential tumor suppressor in solid tumors.
Clinical and molecular characterization of the 20q11.2 microdeletion syndrome: six new patients.
Morin et al., Amiens, France. In Am J Med Genet A, Mar 2015
We have identified a 1.62 megabase minimal critical region involved in this syndrome encompassing three genes—GDF5, EPB41L1, andSAMHD1—which are strong candidates for different aspects of the phenotype.
High-density array comparative genomic hybridization detects novel copy number alterations in gastric adenocarcinoma.
Khayat et al., Belém, Brazil. In Anticancer Res, 2014
(loss of heterozygozity; LOH), where we found LOH of erythrocyte membrane protein band 4.1-like 1 (EPB41L1) gene.
Comprehensive characterization of protein 4.1 expression in epithelium of large intestine.
An et al., Beijing, China. In Histochem Cell Biol, 2014
The protein 4.1 family consists of four members, 4.1R, 4.1N, 4.1B and 4.1G, each encoded by a distinct gene.
The Protein 4.1 family: hub proteins in animals for organizing membrane proteins.
Bennett et al., London, United Kingdom. In Biochim Biophys Acta, 2014
Vertebrates have four paralogues, known as 4.1R, 4.1N, 4.1G and 4.1B, which are additionally duplicated in the ray-finned fish.
Defective expression of Protein 4.1N is correlated to tumor progression, aggressive behaviors and chemotherapy resistance in epithelial ovarian cancer.
Liu et al., Beijing, China. In Gynecol Oncol, 2013
OBJECTIVE: Protein 4.1N (4.1N) is a member of the Protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling.
Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis.
Swanson et al., Chicago, United States. In J Biol Chem, 2013
Here we report that the GluK1 and GluK2 kainate receptor subunits interact with the spectrin-actin binding scaffolding protein 4.1N through a membrane-proximal domain in the C-terminal tail.
The linoleic acid derivative DCP-LA increases membrane surface localization of the α7 ACh receptor in a protein 4.1N-dependent manner.
Nishizaki et al., Nishinomiya, Japan. In Biochem J, 2013
In yeast two-hybrid screening, protein 4.1N, a scaffolding protein, was identified as a binding partner of the α7 ACh (acetylcholine) receptor.
Functional characterization of protein 4.1 homolog in amphioxus: defining a cryptic spectrin-actin-binding site.
Zhang et al., Qingdao, China. In Sci Rep, 2012
We also showed that amphioxus 4.1 protein gene was the common ancestor of vertebrate 4.1 protein genes, from which 4.1R, 4.1N, 4.1G, and 4.1B genes originated.
Proteome analysis of the thalamus and cerebrospinal fluid reveals glycolysis dysfunction and potential biomarkers candidates for schizophrenia.
Turck et al., München, Germany. In J Psychiatr Res, 2010
This protein has been found differentially expressed in thalami from patients with schizophrenia.
The type I inositol 1,4,5-trisphosphate receptor interacts with protein 4.1N to mediate neurite formation through intracellular Ca waves.
Nathanson et al., New Haven, United States. In Neurosignals, 2010
Type I inositol 1,4,5-trisphosphate receptor (IP3R1) localization via protein 4.1N is necessary for divalent calcium ion wave (Ca2+) formation, which in turn mediates neurite formation.
Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation.
Huganir et al., Baltimore, United States. In Nat Neurosci, 2009
study describes a previously unknown mechanism that governs activity-dependent GluR1 trafficking, reveals an interaction between AMPAR palmitoylation and phosphorylation, and underscores the importance of 4.1N in AMPAR trafficking and synaptic plasticity.
Protein 4.1 and the control of ion channels.
Terracciano et al., Canterbury, United Kingdom. In Blood Cells Mol Dis, 2009
4.1R is one member of the mammalian 4.1 family - the others being 4.1N, 4.1G and 4.1B - and is expressed in many cell types other than erythrocytes.
Prefrontal cortex shotgun proteome analysis reveals altered calcium homeostasis and immune system imbalance in schizophrenia.
Turck et al., São Paulo, Brazil. In Eur Arch Psychiatry Clin Neurosci, 2009
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
IP3 receptor/Ca2+ channel: from discovery to new signaling concepts.
Mikoshiba, Wako, Japan. In J Neurochem, 2007
The presence of many kinds of binding partners, like homer, protein 4.1N, huntingtin-associated protein-1A, protein phosphatases (PPI and PP2A), RACK1, ankyrin, chromogranin, carbonic anhydrase-related protein, IRBIT, Na,K-ATPase, and ERp44, suggest that IP(3)Rs form a macro signal complex and function as a center for signaling cascades.
Differential neuronal and glial expression of GluR1 AMPA receptor subunit and the scaffolding proteins SAP97 and 4.1N during rat cerebellar development.
Rubio et al., United States. In J Comp Neurol, 2007
4.1N was expressed postsynaptically at the climbing fibers synapse at early ages during Purkinje cell dendritic growth; its expression changed from neurons to Bergmann glia once these glial cells had completed their enwrapping process.
Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily.
Sikorski et al., Wrocław, Poland. In Folia Histochem Cytobiol, 2005
Non-erythroid cells express the 4.1R homologues: 4.1G (general type), 4.1B (brain type), and 4.1N (neuron type), and the whole group belongs to the protein 4.1 superfamily, which is characterized by the presence of a highly conserved FERM domain at the N-terminus of the molecule.
Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N.
Snyder et al., Baltimore, United States. In Cell, 2001
NGF treatment also leads to PIKE interactions with 4.1N, which has translocated to the nucleus, fitting with the initial identification of PIKE based on its binding 4.1N in a yeast two-hybrid screen.
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