Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Submitted on February 28, 2003
Accepted on May 8, 2003
Translation of Polarity Cues into Asymmetric Spindle Positioning in Caenorhabditis elegans Embryos
Kelly Colombo 1,Stephan W. Grill 2,Randall J. Kimple 3,Francis S. Willard 3,David P. Siderovski 3,Pierre Gönczy 1*
1 Swiss Institute for Experimental Cancer Research (ISREC), 1066 Epalinges/Lausanne, Switzerland. 2 Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany. 3 Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
* To whom correspondence should be addressed. E-mail: pierre.gonczy{at}isrec.unil.ch.
Asymmetric divisions are crucial for generating cell diversityand rely on coupling polarity cues with spindle positioning.How this coupling is achieved is poorly understood. In one-cellstage C. elegans embryos, polarity cues set by the PAR proteinsmediate asymmetric spindle positioning by governing an imbalanceof net pulling forces acting on spindle poles. We found thatthe GoLoco-containing proteins GPR-1 and GPR-2, as well as theG subunits GOA-1 and GPA-16, were essential for generation ofproper pulling forces. GPR-1/2 interacted with GOA-1-GDP andwere enriched on the posterior cortex in a par-3- and par-2-dependentmanner. Thus, the extent of net pulling forces may depend oncortical G activity, which is regulated by anterior-posteriorpolarity cues through GPR-1/2, ensuring coupling between polaritycues and spindle positioning during asymmetric division.
The editors suggest the following Related Resources on Science sites:
Structural Determinants Underlying the Temperature-sensitive Nature of a G{alpha} Mutant in Asymmetric Cell Division of Caenorhabditis elegans.
C. A. Johnston, K. Afshar, J. T. Snyder, G. G. Tall, P. Gonczy, D. P. Siderovski, and F. S. Willard (2008)
J. Biol. Chem.
283, 21550-21558
|Abstract »|Full Text »|PDF »
Interphase microtubule bundles use global cell shape to guide spindle alignment in fission yeast.
A default mechanism of spindle orientation based on cell shape is sufficient to generate cell fate diversity in polarised Xenopus blastomeres.
B. Strauss, R. J. Adams, and N. Papalopulu (2006)
Development
133, 3883-3893
|Abstract »|Full Text »|PDF »
Identification of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbeta{gamma}.
M. Sato, M. J. Cismowski, E. Toyota, A. V. Smrcka, P. A. Lucchesi, W. M. Chilian, and S. M. Lanier (2006)
PNAS
103, 797-802
|Abstract »|Full Text »|PDF »
Cortical localization of the G{alpha} protein GPA-16 requires RIC-8 function during C. elegans asymmetric cell division.
K. Afshar, F. S. Willard, K. Colombo, D. P. Siderovski, and P. Gonczy (2005)
Development
132, 4449-4459
|Abstract »|Full Text »|PDF »
Locomotion defects, together with Pins, regulates heterotrimeric G-protein signaling during Drosophila neuroblast asymmetric divisions.
F. Yu, H. Wang, H. Qian, R. Kaushik, M. Bownes, X. Yang, and W. Chia (2005)
Genes & Dev.
19, 1341-1353
|Abstract »|Full Text »|PDF »
Cleavage furrow formation and ingression during animal cytokinesis: a microtubule legacy.
P. P. D'Avino, M. S. Savoian, and D. M. Glover (2005)
J. Cell Sci.
118, 1549-1558
|Abstract »|Full Text »|PDF »
The RGS14 GoLoco Domain Discriminates among G{alpha}i Isoforms.
The forces that position a mitotic spindle asymmetrically are tethered until after the time of spindle assembly.
J.-C. Labbe, E. K. McCarthy, and B. Goldstein (2004)
J. Cell Biol.
167, 245-256
|Abstract »|Full Text »|PDF »
Identification and Characterization of AGS4: A PROTEIN CONTAINING THREE G-PROTEIN REGULATORY MOTIFS THAT REGULATE THE ACTIVATION STATE OF Gi{alpha}.
X. Cao, M. J. Cismowski, M. Sato, J. B. Blumer, and S. M. Lanier (2004)
J. Biol. Chem.
279, 27567-27574
|Abstract »|Full Text »|PDF »
AGS3 and Signal Integration by G{alpha}s- and G{alpha}i-coupled Receptors: AGS3 BLOCKS THE SENSITIZATION OF ADENYLYL CYCLASE FOLLOWING PROLONGED STIMULATION OF A G{alpha}i-COUPLED RECEPTOR BY INFLUENCING PROCESSING OF G{alpha}i.
M. Sato, T. W. Gettys, and S. M. Lanier (2004)
J. Biol. Chem.
279, 13375-13382
|Abstract »|Full Text »|PDF »
Thermodynamic Characterization of the Binding of Activator of G Protein Signaling 3 (AGS3) and Peptides Derived from AGS3 with G{alpha}i1.