ArticlePloS one2012
Dimerization of DOCK2 is essential for DOCK2-mediated Rac activation and lymphocyte migration.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Integrated Studies on the Biological Functions and Regulatory Mechanisms of Dedicator of Cytokinesis Family Proteins-Secondary Publication.JMA journal · 2026Review
- Heterozygous variants in DOCK2 leading to susceptibility to viral illnesses.The Journal of allergy and clinical immunology · 2026Article
- A hypothesis and evidence map for neuroimmune regulation of DOCK-family cytoskeletal programs in solid tumors.Frontiers in immunology · 2026Review
- DOCK2 Deficiency Causes Defects in Antiviral T-Cell Responses and Impaired Control of Herpes Simplex Virus Infection.The Journal of infectious diseases · 2024Article
- Sulfotransferase 2B1b, Sterol Sulfonation, and Disease.Pharmacological reviews · 2023Review
- Insights from DOCK2 in cell function and pathophysiology.Frontiers in molecular biosciences · 2022Review
- Cryo-EM structure of the human ELMO1-DOCK5-Rac1 complex.Science advances · 2021Article
- A conserved PI(4,5)P2-binding domain is critical for immune regulatory function of DOCK8.Life science alliance · 2021Article
- DOCK family proteins: key players in immune surveillance mechanisms.International immunology · 2020Review
- DOCK2 Sets the Threshold for Entry into the Virtual Memory CD8Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- The carboxy-terminal region of the TBC1D4 (AS160) RabGAP mediates protein homodimerization.International journal of biological macromolecules · 2017Article
- The focal adhesion-associated proteins DOCK5 and GIT2 comprise a rheostat in control of epithelial invasion.Oncogene · 2017Article
- A Rac/Cdc42 exchange factor complex promotes formation of lateral filopodia and blood vessel lumen morphogenesis.Nature communications · 2015Article
- New insights into the dimerization of small GTPase Rac/ROP guanine nucleotide exchange factors in rice.Plant signaling & behavior · 2015Article
- Dock protein family in brain development and neurological disease.Communicative & integrative biology · 2013Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The migratory properties of lymphocytes depend on DOCK2, an atypical Rac activator predominantly expressed in hematopoietic cells. Although DOCK2 does not contain the Dbl homology domain typically found in guanine nucleotide exchange factors (GEFs), DOCK2 mediates the GTP-GDP exchange reaction for Rac via its DOCK homology region (DHR)-2 (also known as CZH2 or Docker) domain. DOCK2 DHR-2 domain is composed of three lobes, and Rac binding site and catalytic center are generated entirely from lobes B and C. On the other hand, lobe A has been implicated in dimer formation, yet its physiological significance remains unknown. Here, we report that lobe A-mediated DOCK2 dimerization is crucial for Rac activation and lymphocyte migration. We found that unlike wild-type DOCK2, DOCK2 mutant lacking lobe A failed to restore motility and polarity when expressed in thymoma cells and primary T cells lacking endogenous expression of DOCK2. Similar results were obtained with the DOCK2 point mutant having a defect in dimerization. Deletion of lobe A from the DHR-2 domain did not affect Rac GEF activity in vitro. However, fluorescence resonance energy transfer analyses revealed that lobe A is required for DOCK2 to activate Rac effectively during cell migration. Our results thus indicate that DOCK2 dimerization is functionally important under the physiological condition where only limited amounts of DOCK2 and Rac are localized to the plasma membrane.
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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.