ATL2 — LLMpedia

Contents

ATL2

Introduction

ATL2 is a member of the atlastin family of dynamin-like GTPases involved in endoplasmic reticulum membrane dynamics. The protein has been discussed alongside work from groups at Harvard University, Massachusetts Institute of Technology, Stanford University, Max Planck Society, and University of California, San Francisco and appears in studies connected to Alzheimer's disease, Parkinson's disease, hereditary spastic paraplegia, axonopathy research, and cellular trafficking research. ATL2 research has intersected with efforts by institutions such as the National Institutes of Health, European Molecular Biology Laboratory, Broad Institute, Cold Spring Harbor Laboratory, and journals like Nature, Cell, and Science.

The ATL2 gene resides on chromosome region 14q32.2 and encodes a ~558 amino acid protein belonging to the atlastin GTPase family that includes paralogs studied at University of Cambridge and University College London. The ATL2 protein contains an N-terminal GTPase domain, a three-helix bundle middle domain, two closely spaced transmembrane helices, and a C-terminal amphipathic tail, a topology characterized in structural studies from teams at EMBL and European Synchrotron Radiation Facility. High-resolution structural models were compared with crystal structures of related GTPases from University of Oxford groups and cryo-EM analyses performed by researchers at University of California, Berkeley and Johns Hopkins University. Sequence conservation and motif mapping referenced datasets from UniProt, Ensembl, GenBank, and comparative genomics initiatives at Wellcome Sanger Institute and Broad Institute.

ATL2 mediates homotypic fusion of endoplasmic reticulum (ER) membranes, cooperating with paralogs whose cellular roles were delineated by labs at Yale University and Columbia University. ATL2-driven membrane fusion influences ER network morphology, and this activity is linked to observations in studies from University of Pennsylvania, University of Chicago, and Northwestern University on organelle connectivity and calcium signaling pathways investigated by teams at Johns Hopkins University School of Medicine. Work intersecting with Drosophila melanogaster genetics from University of Cambridge and The Rockefeller University highlighted conserved roles in neuronal development and axon maintenance alongside models used by Max Planck Institute of Neurobiology.

Variants in atlastin family members have been implicated in neurological disorders; although ATL2 itself is less frequently mutated in clinical cohorts compared to genes reported by researchers at Mayo Clinic and Mount Sinai Health System, ATL2 expression and dysfunction have been evaluated in contexts such as hereditary spastic paraplegia studies at University of Erlangen and University of Freiburg, neuropathy research at Massachusetts General Hospital, and neurodegeneration cohorts investigated by Karolinska Institutet and Queen Square clinicians. ATL2 has been assessed in molecular pathology projects at Memorial Sloan Kettering Cancer Center and in proteomic screens conducted at Scripps Research and Rudolf Magnus Institute, with implications for ER stress-related conditions examined by groups at University of Toronto and University of Sydney.

ATL2 interacts with ER-shaping proteins and membrane fusion factors identified in interaction maps from BioGRID and IntAct and validated by laboratories at University of Geneva and Ludwig Maximilian University of Munich. Identified partners include reticulons characterized at Max Planck Institute for Molecular Cell Biology and Genetics, REEP proteins studied at University of California, San Diego, and other atlastin paralogs analyzed by researchers at University of Basel. Post-translational regulation via phosphorylation and ubiquitination was reported in high-throughput studies at European Bioinformatics Institute and ProteomeXchange contributors, with regulatory kinases and E3 ligases explored in functional screens by teams at Imperial College London and John Innes Centre. ATL2 GTPase activity and dimerization dynamics were quantified in biochemical assays from groups at Cold Spring Harbor Laboratory, Massachusetts Institute of Technology, and ETH Zurich.

ATL2 function has been probed with cellular models such as human induced pluripotent stem cell lines developed at Karolinska Institutet and patient-derived neurons used by labs at University College London and Harvard Medical School. Model organisms including Drosophila, Caenorhabditis elegans, and zebrafish used at Max Planck Institutes and Stowers Institute for Medical Research provided in vivo insights. Techniques applied to ATL2 studies include CRISPR/Cas9 gene editing workflows popularized by teams at Broad Institute and MIT, cryo-electron microscopy methods refined at EMBL-EBI and Pacific Northwest National Laboratory, super-resolution microscopy approaches from Wyss Institute and National Institute of Health intramural researchers, and mass spectrometry proteomics from Scripps Research and Cold Spring Harbor Laboratory. Biochemical reconstitution of membrane fusion used liposome assays established by scientists at University of California, San Diego and University of Illinois Urbana-Champaign.

Category:Human proteins