ArticleScience signaling2016
A large Rab GTPase encoded by CRACR2A is a component of subsynaptic vesicles that transmit T cell activation signals.
Article in Science signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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.
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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
25 citing papers in PubMed, 45 citations in OpenAlex.
- Uncovering protein prenylation in Th1 cells: novel prenylation sites and insights into statin and farnesyltransferase inhibition.BMC biology · 2025Article
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Neutrophil CRACR2A Promotes Neutrophil Recruitment in Sterile Inflammation and Ischemic Stroke.Circulation · 2025Article
- RNA-seq analysis reveals transcriptome changes in livers fromBiochemistry and biophysics reports · 2025Article
- The interplay between hormonal vitamin D and lipopolysaccharide signaling on human neutrophil transcriptional responses.Frontiers in immunology · 2025Article
- The meiotic LINC complex component KASH5 is an activating adaptor for cytoplasmic dynein.The Journal of cell biology · 2023Article
- Organ and cell-specific biomarkers of Long-COVID identified with targeted proteomics and machine learning.Molecular medicine (Cambridge, Mass.) · 2023Article
- Review
- CaJournal of immunology (Baltimore, Md. : 1950) · 2022Article
- Biallelic mutations ineLife · 2021Article
- Large Rab GTPases: Novel Membrane Trafficking Regulators with a Calcium Sensor and Functional Domains.International journal of molecular sciences · 2021Review
- Affinity-based proteomics reveals novel binding partners for Rab46 in endothelial cells.Scientific reports · 2021Article
- Cytoskeletal Transport, Reorganization, and Fusion Regulation in Mast Cell-Stimulus Secretion Coupling.Frontiers in cell and developmental biology · 2021Review
- Rab family of small GTPases: an updated view on their regulation and functions.The FEBS journal · 2021Review
- Role of the EF-hand and coiled-coil domains of human Rab44 in localisation and organelle formation.Scientific reports · 2020Article
- The orphan solute carrier SLC10A7 is a novel negative regulator of intracellular calcium signaling.Scientific reports · 2020Article
- CaHeliyon · 2020Article
- microRNA-519d Induces Autophagy and Apoptosis of Human Hepatocellular Carcinoma Cells Through Activation of the AMPK Signaling Pathway via Rab10.Cancer management and research · 2020Article
- Rab46 integrates CaThe Journal of cell biology · 2019Article
- CRACR2a is a calcium-activated dynein adaptor protein that regulates endocytic traffic.The Journal of cell biology · 2019Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
More than 60 members of the Rab family of guanosine triphosphatases (GTPases) exist in the human genome. Rab GTPases are small proteins that are primarily involved in the formation, trafficking, and fusion of vesicles. We showed thatCRACR2A(Ca(2+) release-activated Ca(2+) channel regulator 2A) encodes a lymphocyte-specific large Rab GTPase that contains multiple functional domains, including EF-hand motifs, a proline-rich domain (PRD), and a Rab GTPase domain with an unconventional prenylation site. Through experiments involving gene silencing in cells and knockout mice, we demonstrated a role for CRACR2A in the activation of the Ca(2+) and c-Jun N-terminal kinase signaling pathways in response to T cell receptor (TCR) stimulation. Vesicles containing this Rab GTPase translocated from near the Golgi to the immunological synapse formed between a T cell and a cognate antigen-presenting cell to activate these signaling pathways. The interaction between the PRD of CRACR2A and the guanidine nucleotide exchange factor Vav1 was required for the accumulation of these vesicles at the immunological synapse. Furthermore, we demonstrated that GTP binding and prenylation of CRACR2A were associated with its localization near the Golgi and its stability. Our findings reveal a previously uncharacterized function of a large Rab GTPase and vesicles near the Golgi in TCR signaling. Other GTPases with similar domain architectures may have similar functions in T cells.
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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.