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ER lipid raft associated 2

SPFH2, C8orf2, erlin2
This gene encodes a member of the SPFH domain-containing family of lipid raft-associated proteins. The encoded protein is localized to lipid rafts of the endoplasmic reticulum and plays a critical role in inositol 1,4,5-trisphosphate (IP3) signaling by mediating ER-associated degradation of activated IP3 receptors. Mutations in this gene are a cause of spastic paraplegia-18 (SPG18). Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: fibrillin-1, prohibitin, ACID, CAN, OUT
Papers on SPFH2
The stromal cell-surface protease fibroblast activation protein-α localizes to lipid rafts and is recruited to invadopodia.
Schilling et al., Freiburg, Germany. In Biochim Biophys Acta, Oct 2015
Complex formation with adenosin deaminase, erlin-2, stomatin, prohibitin, Thy-1 membrane glycoprotein, and caveolin-1 was further validated by immunoblotting.
Arsenite-induced changes in hepatic protein abundance in cynomolgus monkeys (Macaca fascicularis).
Ryu et al., Seoul, South Korea. In Proteomics, 2014
Specifically, the levels of two proteins, mortalin and tubulin beta chain, were increased, and 14 were decreased, including plastin-3, cystathionine-beta-synthase, selenium-binding protein 1, annexin A6, alpha-enolase, phosphoenolpyruvate carboxykinase-M, erlin-2, and arginase-1.
Proteomic analysis of detergent resistant membrane domains during early interaction of macrophages with rough and smooth Brucella melitensis.
Boyle et al., Blacksburg, United States. In Plos One, 2013
For some of the proteins such as myosin 9, small G protein signaling modulator 3, lysine-specific demethylase 5D, erlin-2, and voltage-dependent anion-selective channel protein 2, we observed extreme differential depletion or enrichment in DRMDs.
Hereditary spastic paraplegia: clinico-pathologic features and emerging molecular mechanisms.
Fink, Ann Arbor, United States. In Acta Neuropathol, 2013
SPG2/Proteolipid protein and SPG42/Connexin 47); (5) protein folding and ER-stress response (SPG6/NIPA1, SPG8/K1AA0196 (Strumpellin), SGP17/BSCL2 (Seipin), "mutilating sensory neuropathy with spastic paraplegia" owing to CcT5 mutation and presumably SPG18/ERLIN2); (6) corticospinal tract and other neurodevelopment (e.g.
A novel splice site mutation in ERLIN2 causes hereditary spastic paraplegia in a Saudi family.
Al-Hassnan et al., Riyadh, Saudi Arabia. In Eur J Med Genet, 2013
An intronic splice acceptor site mutation in ERLIN2 was found to be responsible for causing this disorder found in this family.
Loss of ERLIN2 function leads to juvenile primary lateral sclerosis.
Al-Mohanna et al., Riyadh, Saudi Arabia. In Ann Neurol, 2012
In this study, we identify mutation of the ERLIN2 gene in juvenile PLS patients and describe an in vitro model for loss of ERLIN2 function.
Endoplasmic reticulum factor ERLIN2 regulates cytosolic lipid content in cancer cells.
Zhang et al., Detroit, United States. In Biochem J, 2012
a novel role for ERLIN2 in supporting cancer cell growth by promoting the activation of the key lipogenic regulator SREBP1c and the production of cytosolic lipid droplets.
Erlin-2 is associated with active γ-secretase in brain and affects amyloid β-peptide production.
Tjernberg et al., Stockholm, Sweden. In Biochem Biophys Res Commun, 2012
a novel brain gamma-secretase associated protein , erlin-2, that resides in detergent resistant membranes and affects amyloid beta-peptide production.
Hereditary spastic paraplegias with autosomal dominant, recessive, X-linked, or maternal trait of inheritance.
Stevanin et al., Vienna, Austria. In J Neurol Sci, 2012
Among the AR-SPGs, ~20% of the patients carry mutations in the KIAA1840 (SPG11) gene whereas the 15 other genes are rarely mutated and account for SPGs in single families yet (CYP7B1 (SPG5), SPG7 (SPG7), ZFYVE26 (SPG15), ERLIN2 (SPG18), SPG20 (SPG20), ACP33 (SPG21), KIF1A (SPG30), FA2H (SPG35), NTE (SPG39), GJA12/GJC2 (SPG44), KIAA0415 (SPG48) and 4 genes encoding for the AP4-complex (SPG47)).
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
ERLIN2 promotes breast cancer cell survival by modulating endoplasmic reticulum stress pathways.
Yang et al., Detroit, United States. In Bmc Cancer, 2011
Previous genomic analysis has led us to identify the endoplasmic reticulum (ER) lipid raft-associated 2 (ERLIN2) gene as one of the candidate oncogenes within the 8p11-12 amplicon in human breast cancer, particularly in the luminal subtype.
Proteomic analysis of lipid raft-enriched membranes isolated from internal organelles.
Bazemore-Walker et al., Providence, United States. In Biochem Biophys Res Commun, 2011
Most importantly, known internal LR marker proteins (inositol 1,4,5-trisphosphate receptor type 3, erlin-2, and voltage-dependent anion channel 1) were detected as well as most of the components of the mitochondrial/MAM-localized Ca(2+) signaling complex.
Clustered hydrophobic amino acids in amphipathic helices mediate erlin1/2 complex assembly.
Wojcikiewicz et al., Syracuse, United States. In Biochem Biophys Res Commun, 2011
Erlin1 and erlin2 are highly homologous, ∼40kDa, endoplasmic reticulum membrane proteins that assemble into a ring-shaped complex with a mass of ∼2 MDa.
A nullimorphic ERLIN2 mutation defines a complicated hereditary spastic paraplegia locus (SPG18).
Alkuraya et al., Riyadh, Saudi Arabia. In Neurogenetics, 2011
study describes an extended consanguineous Saudi family in which hereditary spastic paraplegia is linked to SPG18, an autosomal recessive locus, and show it is associated with a nullimorphic deletion of ERLIN2
A frameshift mutation of ERLIN2 in recessive intellectual disability, motor dysfunction and multiple joint contractures.
Tolun et al., İstanbul, Turkey. In Hum Mol Genet, 2011
The gene encodes endoplasmic reticulum (ER) lipid raft-associated protein 2 that mediates the ER-associated degradation of activated inositol 1,4,5-trisphosphate receptors and other substrates.
Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
DeBose-Boyd et al., Dallas, United States. In J Biol Chem, 2011
Here, we identify two ER membrane proteins, SPFH2 and TMUB1, as associated proteins of mammalian gp78, a membrane-bound ubiquitin ligase that bears significant sequence homology with mammalian Hrd1 and mediates sterol-accelerated ERAD of the cholesterol biosynthetic enzyme HMG-CoA reductase.
When worlds collide: IP(3) receptors and the ERAD pathway.
Wang et al., Syracuse, United States. In Cell Calcium, 2009
Here we review recent studies showing that activated IP(3) receptors are ubiquitinated in an unexpectedly complex manner, and that a novel complex composed of the ER membrane proteins SPFH1 and SPFH2 (erlin 1 and 2) binds to IP(3) receptors immediately after they are activated and mediates their ERAD.
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