CED-12/ELMO, a Novel Member of the CrkII/Dock180/Rac Pathway, Is Required for Phagocytosis and Cell Migration

@article{Gumienny2001CED12ELMOAN,
  title={CED-12/ELMO, a Novel Member of the CrkII/Dock180/Rac Pathway, Is Required for Phagocytosis and Cell Migration},
  author={Tina L. Gumienny and Enrico Brugnera and Annie-Carole Tosello-Trampont and Jason Michael Kinchen and Lisa B. Haney and Kiyoji Nishiwaki and Scott F. Walk and Michael E Nemergut and Ian G. Macara and Ross Francis and Tim Schedl and Yi Qin and Linda van Aelst and Michael O. Hengartner and Kodi S. Ravichandran},
  journal={Cell},
  year={2001},
  volume={107},
  pages={27-41}
}
View on Elsevier
cell.com
533 Citations
Highly Influential Citations
23
Background Citations
166
Methods Citations
3
Results Citations
5

Figures and Tables from this paper

533 Citations

Citation Type

Citation Type

C. elegans CED-12 acts in the conserved crkII/DOCK180/Rac pathway to control cell migration and cell corpse engulfment.
The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway.
Two pathways converge at CED-10 to mediate actin rearrangement and corpse removal in C. elegans
TLDR
It is shown that CED-1, C-6 and C-7 are required for actin reorganization around the apoptotic cell corpse, and that C-10(Rac) GTPase acts genetically downstream of these proteins to mediate corpse removal, functionally linking the two engulfment pathways and identifying the CED, -6 and -7 signalling module as upstream regulators of Rac activation.
Phagocytosis of Apoptotic Cells Is Regulated by a UNC-73/TRIO-MIG-2/RhoG Signaling Module and Armadillo Repeats of CED-12/ELMO
Identification of two signaling submodules within the CrkII/ELMO/Dock180 pathway regulating engulfment of apoptotic cells
TLDR
Functional studies in cell lines suggest that Dock180/ELMO and CrkII act as two evolutionarily conserved signaling submodules that coordinately regulate engulfment.
Interaction of CED-6/GULP, an Adapter Protein Involved in Engulfment of Apoptotic Cells with CED-1 and CD91/Low Density Lipoprotein Receptor-related Protein (LRP)*
TLDR
Evidence is presented for a physical link between CED-1 or CD91/LRP and the adapter protein C ED-6/GULP during engulfment of apoptotic cells and further elucidate the pathway suggested by the genetic studies.
Dock180 and ELMO1 Proteins Cooperate to Promote Evolutionarily Conserved Rac-dependent Cell Migration*
TLDR
This finding suggests that Rac activation by the ELMO·Dock180 complex at discrete intracellular locations mediated by the N-terminal 330 amino acids of ELMO1 rather than generalized Rac activation plays a role in cell migration.
BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module
TLDR
It is shown that BAI1 functions as an engulfment receptor in both the recognition and subsequent internalization of apoptotic cells, and is a phosphatidylserine recognition receptor that can directly recruit a Rac–GEF complex to mediate the uptake of apoptosis cells.
C‐terminal SH3 domain of CrkII regulates the assembly and function of the DOCK180/ELMO Rac‐GEF
TLDR
It is found that mutations that disrupt the C‐terminal SH3 domain of CrkII (CrkII‐SH3‐C) abrogate engulfment of apoptotic cells and impair cell spreading on extracellular matrix, and studies with W276K Crk II may offer a unique opportunity to study the structure and function of the DOCK180/ELMO Rac‐GEF.
The Drosophila TRPP Cation Channel, PKD2 and Dmel/Ced-12 Act in Genetically Distinct Pathways during Apoptotic Cell Clearance
TLDR
It is proposed that PKD2 functions in the DRPR/RTP pathway to regulate calcium homeostasis during phagocytosis during this process, and appears to function in a genetically distinct pathway.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 83 REFERENCES
CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans
TLDR
It is proposed that CED-2/CrkII and Ced-5/DOCK180 function to activate CED -10/Rac in a GTPase signalling pathway that controls the polarized extension of cell surfaces.
Evidence for a Conserved Role for CrkII and Rac in Engulfment of Apoptotic Cells*
TLDR
CED-2/CrkII and CED-10/Rac are part of an evolutionarily conserved pathway in engulfment of apoptotic cells, which is consistent with genetic studies in the worm that place ced-10 downstream ofced-2 (crk) in cell corpse removal.
CED-1 Is a Transmembrane Receptor that Mediates Cell Corpse Engulfment in C. elegans
Candidate Adaptor Protein CED-6 Promotes the Engulfment of Apoptotic Cells in C. elegans
C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180
TLDR
This work reports that ced-5, a gene required for cell-corpse engulfment in the nematode Caenorhabditis elegans, encodes a protein that is similar to the human protein DOCK180 and the Drosophila melanogaster protein Myoblast City, both of which have been implicated in the extension of cell surfaces.
αvβ5 integrin recruits the CrkII–Dock180–Rac1 complex for phagocytosis of apoptotic cells
TLDR
The αvβ5 receptor mediates both binding and internalization of apoptotic cells and is linked to the CrkII–Dock180–Rac1 molecular complex in mammalian cells, revealing an evolutionarily conserved signalling pathway that is responsible for the recognition and internalized of apoptosis by both professional and non-professional phagocytes.
Requirement for Rho GTPases and PI 3-kinases during apoptotic cell phagocytosis by macrophages
The C. elegans Cell Corpse Engulfment Gene ced-7 Encodes a Protein Similar to ABC Transporters
CAS/Crk Coupling Serves as a “Molecular Switch” for Induction of Cell Migration
TLDR
CAS/Crk assembly serves as a “molecular switch” for the induction of cell migration and appears to contribute to the invasive property of tumors.
Myoblast city, the Drosophila homolog of DOCK180/CED-5, is required in a Rac signaling pathway utilized for multiple developmental processes.
TLDR
Results suggest that Mbc is a specific upstream regulator of Rac activity that mediates several morphogenetic processes in Drosophila embryogenesis.
...
1
2
3
4
5
...