Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin.
Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners.
Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance.
Mutations in the SPG3A gene encoding the GTPase atlastin interfere with vesicle trafficking in the ER/Golgi interface and Golgi morphogenesis.
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The original abstract reports ER as well as Golgi and neuronal-process localization.
"Atlastin is
localized in the endoplasmic reticulum, the Golgi, neurites and growth cones"
A class of dynamin-like GTPases involved in the generation of the tubular ER network.
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The family-level abstract reports tubular ER localization and a network-formation requirement; target-specific experiments are separately described in the source reading notes.
"The
atlastins localize to the tubular ER and are required for proper network
formation in vivo and in vitro."
Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network.
Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A.
Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes.
Structural basis for conformational switching and GTP loading of the large G protein atlastin.
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The cytoplasmic atlastin domain supplies nucleotide-timed tethering and self-association.
"the cytoplasmic domain of atlastin
acts as a tether and homotypic interactions are timed by GTP binding and
hydrolysis."
Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation.
Mutation in CPT1C Associated With Pure Autosomal Dominant Spastic Paraplegia.
Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons to generate a tubular membrane network.
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ATL activity supports ER-network maintenance as well as initial formation.
"ATL is
needed to not only form, but also maintain, the ER network."
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dissecting the mechanism of atlastin-mediated homotypic membrane fusion at the single-molecule level.
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The study distinguishes two disease-associated human substitutions from its engineered proline mutant.
"two disease-causing
mutations affect human ATL1 activity by destabilizing GTP binding-induced loose
crossover dimer formation and the membrane-embedded helix, respectively."
Reconstitution of human atlastin fusion activity reveals autoinhibition by the C terminus.