Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization.
ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter.
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Predominantly cytosolic ARL2BP also has a mitochondrial pool.
"Both ARL2 and BART are predominantly cytosolic, but a
pool of each was found associated with mitochondria in a protease-resistant
form."
Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C.
Arl2 and Arl3 regulate different microtubule-dependent processes.
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Controlled staining detects centrosomal ARL2BP.
"Arl2 or Bart staining at centrosomes was evident in a wide range of cell lines (including CHO, NIH3T3, HEK, Sf295, and HeLa cells)"
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Bart spindle and midbody patterns differ under the tested conditions.
"Bart staining was absent from the spindle but was found in the midbody"
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Specific BART staining supports access to the nucleus.
"Nuclear staining with Bart antisera was also observed after methanol fixation though this was often quite weak in intensity."
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The localization study concludes that the proteins, including BART, access nucleoplasm.
"Thus, we conclude that all three of the proteins under study can access the nucleoplasm."
BART is essential for nuclear retention of STAT3.
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ARL2BP binds STAT3 and supports its nuclear retention.
"we identified binder of ADP-ribosylation factor-like two (BART)
as a novel STAT-binding partner."
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ARL2 contributes to the nuclear-retention mechanism.
"BART plays an essential
role in the nuclear retention of STAT3 through interaction with ARL2."
Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.
Toward an understanding of the protein interaction network of the human liver.
A proteome-scale map of the human interactome network.
A massively parallel pipeline to clone DNA variants and examine molecular phenotypes of human disease mutations.
The Interaction of CCDC104/BARTL1 with Arl3 and Implications for Ciliary Function.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
ARL2:GTP:ARL2BP binds SLC25A4
ARL2:GTP:ARL2BP translocates from cytosol to the mitochondrial matrix
ARL2:GTP:ARL2BP:SLC25A4 dimer exchanges ATP for ADP across the mitochondrial inner membrane
Mutations in ARL2BP, encoding ADP-ribosylation-factor-like 2 binding protein, cause autosomal-recessive retinitis pigmentosa.
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The disease-associated ARL2BP substitution disrupts basal-body localization in human nasal epithelial cells.
"the p.Met45Arg amino acid
substitution reduced binding to ARL2 and caused the loss of ARL2BP localization
at the basal body in ciliated nasal epithelial cells."
ARL2BP, a protein linked to retinitis pigmentosa, is needed for normal photoreceptor cilia doublets and outer segment structure.
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Arl2bp-null mouse photoreceptors have defective doublet microtubule architecture.
"However, most strikingly, animals lacking ARL2BP displayed abnormal DMT organization, with multiple MTs possessing open B-tubules (Figure 6A)."
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The reconstituted ARL2 interaction was not recovered in the tested photoreceptor experiments.
"However, our attempts to confirm this interaction in photoreceptors have so far been unproductive (Supplemental Figure 10)."
Mutations in ARL2BP, a protein required for ciliary microtubule structure, cause syndromic male infertility in humans and mice.
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The early cilium-resorption delay in knockout mouse fibroblasts is not a persistent late block.
"Further observation of KO and WT MEFs revealed that cilia resorption was not statistically different between them from 6 to 24 hours (Fig 10D)."
ARL3 activation requires the co-GEF BART and effector-mediated turnover.
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BART cooperates with ARL13B in ARL3 nucleotide exchange independently of product trapping.
"The presence of BART is able to accelerate and increase the nucleotide exchange of ARL3mantGDP with unlabelled GDP, excluding the necessity of binding to the product, ARL3GTP, to accelerate the dissociation of the bound GDP (Figure 3B)."
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BART stabilizes GTP-bound ARL3 by limiting nucleotide dissociation.
"BART binds to ARL3GTP and inhibits the dissociation of the otherwise relatively fast dissociating GTP (Figure 5B)."
ARL2BP primary-source assessment and functional synthesis
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Original human BART comparator assays establish ARL2 and ARL3 association.
"The original PMID:11847227 human BART positive-control pull-down experiments directly support association with both ARL2 and ARL3. They do not assign the RP2 tubulin-GAP activity to BART."
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Original depletion and vanadate observations support STAT3 phosphorylation regulation.
"In the original PMID:18234692 Results, BART depletion reduces STAT3 tyrosine phosphorylation, and vanadate sustains phosphorylation in the depleted cells. This supports a regulatory contribution without establishing kinase activity of BART."
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Original SOCS3 and reporter observations support context-dependent transcriptional regulation.
"In the original PMID:18234692 Results, BART depletion reduces IL-6-induced SOCS3 mRNA in Hep3B cells and LIF-dependent reporter output in HeLa cells. These observations support context-dependent transcriptional regulation without demonstrating BART action at a genomic locus."