ArticlePloS one2013
The immune system GTPase GIMAP6 interacts with the Atg8 homologue GABARAPL2 and is recruited to autophagosomes.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Comparative Transcriptomic Analysis of Human Macrophages During Mycobacterium avium Versus Mycobacterium tuberculosis Infection.Molecular microbiology · 2026Article
- Upregulated small GTPase immunity-associated proteins confer resistance toFrontiers in cellular and infection microbiology · 2025Article
- GIMAP5 deficiency reveals a mammalian ceramide-driven longevity assurance pathway.Nature immunology · 2024Article
- Attenuation of In Vitro and In Vivo Virulence Is Associated with Repression of Gene Expression of AIG1 Gene inPathogens (Basel, Switzerland) · 2023Article
- GIMAP6 regulates autophagy, immune competence, and inflammation in mice and humans.The Journal of experimental medicine · 2022Article
- Unlocking the gate to GABARAPL2.Biologia futura · 2022Review
- Patchy Distribution of GTPases of Immunity-Associated Proteins (GIMAP) within Cnidarians and Dinoflagellates Suggests a Complex Evolutionary History.Genome biology and evolution · 2022Article
- MON-2, a Golgi protein, mediates autophagy-dependent longevity inScience advances · 2021Article
- The GIMAP Family Proteins: An Incomplete Puzzle.Frontiers in immunology · 2021Review
- MicroRNA and mRNA analysis of angiotensin II-induced renal artery endothelial cell dysfunction.Experimental and therapeutic medicine · 2020Article
- Effects of hub genes on the clinicopathological and prognostic features of lung adenocarcinoma.Oncology letters · 2020Article
- Genetic Factors Mediate the Impact of Chronic Stress and Subsequent Response to Novel Acute Stress.Frontiers in neuroscience · 2019Article
- Small GTPase Immunity-Associated Proteins Mediate Resistance to Toxoplasma gondii Infection in Lewis Rat.Infection and immunity · 2018Article
- Article
- Functional and biochemical characterization of a T cell-associated anti-apoptotic protein, GIMAP6.The Journal of biological chemistry · 2017Article
- Integrative analysis of pathway deregulation in obesity.NPJ systems biology and applications · 2017Article
- GTPase of the Immune-Associated Nucleotide Protein 5 Regulates the Lysosomal Calcium Compartment in T Lymphocytes.Frontiers in immunology · 2017Article
- Dysregulation of GTPase IMAP family members in hepatocellular cancer.Molecular medicine reports · 2016Article
- Tubulin- and actin-associating GIMAP4 is required for IFN-γ secretion during Th cell differentiation.Immunology and cell biology · 2015Article
- Multiple roles of the cytoskeleton in bacterial autophagy.PLoS pathogens · 2014Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The GIMAPs (GTPases of the immunity-associated proteins) are a family of small GTPases expressed prominently in the immune systems of mammals and other vertebrates. In mammals, studies of mutant or genetically-modified rodents have indicated important roles for the GIMAP GTPases in the development and survival of lymphocytes. No clear picture has yet emerged, however, of the molecular mechanisms by which they perform their function(s). Using biotin tag-affinity purification we identified a major, and highly specific, interaction between the human cytosolic family member GIMAP6 and GABARAPL2, one of the mammalian homologues of the yeast autophagy protein Atg8. Chemical cross-linking studies performed on Jurkat T cells, which express both GIMAP6 and GABARAPL2 endogenously, indicated that the two proteins in these cells readily associate with one another in the cytosol under normal conditions. The GIMAP6-GABARAPL2 interaction was disrupted by deletion of the last 10 amino acids of GIMAP6. The N-terminal region of GIMAP6, however, which includes a putative Atg8-family interacting motif, was not required. Over-expression of GIMAP6 resulted in increased levels of endogenous GABARAPL2 in cells. After culture of cells in starvation medium, GIMAP6 was found to localise in punctate structures with both GABARAPL2 and the autophagosomal marker MAP1LC3B, indicating that GIMAP6 re-locates to autophagosomes on starvation. Consistent with this finding, we have demonstrated that starvation of Jurkat T cells results in the degradation of GIMAP6. Whilst these findings raise the possibility that the GIMAPs play roles in the regulation of autophagy, we have been unable to demonstrate an effect of GIMAP6 over-expression on autophagic flux.
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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.