ArticleThe Journal of biological chemistry2012
ELMO domains, evolutionary and functional characterization of a novel GTPase-activating protein (GAP) domain for Arf protein family GTPases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
49 citing papers in PubMed, 66 citations in OpenAlex.
- TBC1D15 functions as an Arl4D GAP and promotes the mitochondrial translocation of Arl4D for organelle homeostasis.Journal of cell science · 2026Article
- Eukaryote-Wide Distribution of a Family of Longin Domain-Containing GAP Complexes for Small GTPases.Traffic (Copenhagen, Denmark) · 2025Article
- ELMO2 is an essential regulator of carotid artery development.Nature communications · 2025Article
- ELMOD2 Overexpression Predicts Adverse Outcomes and Regulates Tumor Progression in Gliomas.Current medical science · 2025Article
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- CED-5/CED-12 (DOCK/ELMO) can promote and inhibit F-actin formation via distinct motifs that may target different GTPases.PLoS genetics · 2024Article
- CED-5/CED-12 (DOCK/ELMO) can promote and inhibit F-actin formation via distinct motifs that target different GTPases.bioRxiv : the preprint server for biology · 2023Article
- The ARF GTPase regulatory network in collective invasion and metastasis.Biochemical Society transactions · 2023Review
- ELMOD3-Rab1A-Flotillin2 cascade regulates lumen formation via vesicle trafficking inOpen biology · 2023Article
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- Role of ELMO1 in inflammation and cancer-clinical implications.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia to regulate ciliogenesis and ciliary protein traffic.Molecular biology of the cell · 2022Article
- Comparative Morphological, Metabolic and Transcriptome Analyses inFrontiers in cell and developmental biology · 2022Article
- Members of the ELMOD protein family specify formation of distinct aperture domains on theeLife · 2021Article
- Small GTPases of the Rab and Arf Families: Key Regulators of Intracellular Trafficking in Neurodegeneration.International journal of molecular sciences · 2021Review
- Roles for ELMOD2 and Rootletin in ciliogenesis.Molecular biology of the cell · 2021Article
- Signaling in the primary cilium through the lens of the Hedgehog pathway.Wiley interdisciplinary reviews. Developmental biology · 2020Review
- The ARF GAP ELMOD2 acts with different GTPases to regulate centrosomal microtubule nucleation and cytokinesis.Molecular biology of the cell · 2020Article
- ARF family GTPases with links to cilia.American journal of physiology. Cell physiology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The human family of ELMO domain-containing proteins (ELMODs) consists of six members and is defined by the presence of the ELMO domain. Within this family are two subclassifications of proteins, based on primary sequence conservation, protein size, and domain architecture, deemed ELMOD and ELMO. In this study, we used homology searching and phylogenetics to identify ELMOD family homologs in genomes from across eukaryotic diversity. This demonstrated not only that the protein family is ancient but also that ELMOs are potentially restricted to the supergroup Opisthokonta (Metazoa and Fungi), whereas proteins with the ELMOD organization are found in diverse eukaryotes and thus were likely the form present in the last eukaryotic common ancestor. The segregation of the ELMO clade from the larger ELMOD group is consistent with their contrasting functions as unconventional Rac1 guanine nucleotide exchange factors and the Arf family GTPase-activating proteins, respectively. We used unbiased, phylogenetic sorting and sequence alignments to identify the most highly conserved residues within the ELMO domain to identify a putative GAP domain within the ELMODs. Three independent but complementary assays were used to provide an initial characterization of this domain. We identified a highly conserved arginine residue critical for both the biochemical and cellular GAP activity of ELMODs. We also provide initial evidence of the function of human ELMOD1 as an Arf family GAP at the Golgi. These findings provide the basis for the future study of the ELMOD family of proteins and a new avenue for the study of Arf family GTPases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.