CED-12/ELMO, a novel member of the crkII/dock180/rac pathway, is required for phagocytosis and cell migration

Gumienny, T. L., Brugnera, E., Tosello-Trampont, A. C., Kinchen, J. M., Haney, L. B., Nishiwaki, K., Walk, S. F., Nemergut, M. E., Macara, I. G., Francis, R., Schedl, T., Qin, Y., Van Aelst, L., Hengartner, M. O., Ravichandran, K. S. (2001) CED-12/ELMO, a novel member of the crkII/dock180/rac pathway, is required for phagocytosis and cell migration. Cell, 107 (1). pp. 27-41. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/11595183
DOI: 10.1016/s0092-8674(01)00520-7

Abstract

The C. elegans genes ced-2, ced-5, and ced-10, and their mammalian homologs crkII, dock180, and rac1, mediate cytoskeletal rearrangements during phagocytosis of apoptotic cells and cell motility. Here, we describe an additional member of this signaling pathway, ced-12, and its mammalian homologs, elmo1 and elmo2. In C. elegans, CED-12 is required for engulfment of dying cells and for cell migrations. In mammalian cells, ELMO1 functionally cooperates with CrkII and Dock180 to promote phagocytosis and cell shape changes. CED-12/ELMO-1 binds directly to CED-5/ Dock180; this evolutionarily conserved complex stimulates a Rac-GEF, leading to Rac1 activation and cytoskeletal rearrangements. These studies identify CED-12/ELMO as an upstream regulator of Rac1 that affects engulfment and cell migration from C. elegans to mammals.

Item Type: Paper
Uncontrolled Keywords: NEMATODE CAENORHABDITIS-ELEGANS C-ELEGANS RHO-GTPASES APOPTOTIC CELLS FAMILY PROTEINS BINDING PROTEIN MYOBLAST CITY ENGULFMENT DOCK180 DEATH
Subjects: organism description > animal > C elegans
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GTPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Rac
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Rho
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Hengartner lab
CSHL labs > Van Aelst lab
Depositing User: Matt Covey
Date Deposited: 18 Dec 2013 22:04
Last Modified: 18 Dec 2013 22:04
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29098

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving