Dock-family exchange factors in cell migration and disease
Abstract
Dock family proteins are evolutionary conserved exchange factors for the Rho GTPases Rac and Cdc42. There are 11 Dock proteins in mammals, named Dock1 (or Dock180) to Dock11 that play different cellular functions. In particular, Dock proteins regulate actin cytoskeleton, cell adhesion and migration. Not surprisingly, members of the Dock family have been involved in various pathologies, including cancer and defects in the central nervous and immune systems. This review proposes an update of the recent findings regarding the function of Dock proteins, focusing on their role in the control of cell migration and invasion and the consequences in human diseases.
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DOCK5-deficient mice, while otherwise healthy, have significantly increased bone mass.
“DOCK5-deficient mice, while otherwise healthy, were characterized by significantly increased bone mass, a classical symptom of improper bone resorption (94).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [94]
DOCK11 is highly expressed in B and T lymphocytes.
“DOCK11 is a CDC42-specific GEF that is highly expressed in B and T lymphocytes and has been shown to participate in B-cell homeostasis and differentiation mechanisms (94, 97, 128).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [94]
DOCK11 participates in B-cell homeostasis and differentiation mechanisms.
“DOCK11 is a CDC42-specific GEF that is highly expressed in B and T lymphocytes and has been shown to participate in B-cell homeostasis and differentiation mechanisms (94, 97, 128).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [94]
DOCK11 is a CDC42-specific GEF.
“DOCK11 is a CDC42-specific GEF that is highly expressed in B and T lymphocytes and has been shown to participate in B-cell homeostasis and differentiation mechanisms (94, 97, 128).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [94]
Cites
Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
Brugnera, E., Haney, L., Grimsley, C., Lu, M., Walk, S. F., Tosello-Trampont, A.-C., Macara, I. G., Madhani, H., Fink, G. R., & Ravichandran, K. S. (2002) · Nature Cell Biology · doi:10.1038/ncb824 · Cited by 576 · see citing works
Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
Fukui, Y., Hashimoto, O., Sanui, T., Oono, T., Koga, H., Abe, M., Inayoshi, A., Noda, M., Oike, M., Shirai, T., et al. (2001) · Nature · doi:10.1038/35090591 · Cited by 449 · see citing works
Cook, D. R., Rossman, K. L., & Der, C. J. (2014) · Oncogene · doi:10.1038/onc.2013.362 · Cited by 378 · see citing works
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
Meller, N., Irani-Tehrani, M., Kiosses, W. B., Del Pozo, M. A., & Schwartz, M. A. (2002) · Nature Cell Biology · doi:10.1038/ncb835 · Cited by 171 · see citing works
Jing, Y.-Y., Han, Z.-P., Sun, K., Zhang, S.-S., Hou, J., Liu, Y., Li, R., Gao, L., Zhao, X., Zhao, Q.-D., et al. (2012) · BMC Medicine · doi:10.1186/1741-7015-10-98 · Cited by 162 · see citing works
Functional Significance of Smad2 in Regulating Basal Keratinocyte Migration During Wound Healing
Hosokawa, R., Urata, M. M., Ito, Y., Bringas, P., & Chai, Y. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23963.x · Cited by 63 · see citing works
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Thompson, A. P., Bitsina, C., Gray, J. L., von Delft, F., & Brennan, P. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100521 · Cited by 21 · see citing works
“DOCK11 is a CDC42-specific GEF that is highly expressed in B and T lymphocytes and has been shown to participate in B-cell homeostasis and differentiation mechanisms (94, 97, 128).”
Background
- Authors
- Gadea, G., & Blangy, A.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Blangy, Anne
- ORCID
- Blangy, Anne
- Venue
- European Journal of Cell Biology
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 93
- Issue
- 10-12
- Pages
- 466-477
- ISSN
- 0171-9335 (ISSN-L)
- OpenAlex
- W2062667529
- Cited by
- 217
- References
- 6
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 23 · 2023: 11 · 2022: 25 · 2021: 37 · 2020: 18 · 2019: 24 · 2018: 15 · 2017: 18 · 2016: 14 · 2015: 7 · 2014: 1
- FWCI
- 1.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National du Cancer (INCa-4361)
- Agence Nationale de la Recherche (ANR-2011-BLAN-006)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Rac, Cdc42, cell migration, cell invasion, actin cytoskeleton, cell adhesion, cancer, central nervous system disorders, immune disorders
- MeSH terms
- Animals, Axons, Bone Resorption, Cell Adhesion, Cell Movement, Humans, Immune System, Actin Cytoskeleton, Neoplasm Invasiveness, Neoplasms, Osteoclasts, Signal Transduction, Guanine Nucleotide Exchange Factors, rho GTP-Binding Proteins, cdc42 GTP-Binding Protein
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