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Previous Article | Next Article
Volume 17, Number 16, Issue of August 15, 1997 pp. 6256-6263
Copyright ©1997 Society for NeuroscienceRac1 Mediates Collapsin-1-Induced Growth Cone Collapse
Received March 18, 1997; revised May 14, 1997; accepted May 23, 1997.
Zhao Jin and Stephen M. Strittmatter Departments of Neurology and Neurobiology, Yale University School of Medicine, New Haven, Connecticut 06520
Collapsin-1 or semaphorin III(D) inhibits axonal outgrowth by collapsing the lamellipodial and filopodial structures of the neuronal growth cones. Because growth cone collapse is associated with actin depolymerization, we considered whether small GTP-binding proteins of the rho subfamily might participate in collapsin-1 signal transduction. Recombinant rho, rac1, and cdc42 proteins were triturated into embryonic chick (DRG) neurons. Constitutively active rac1 increases the proportion of collapsed growth cones, and dominant negative rac1 inhibits collapsin-1-induced collapse of growth cones and collapsin-1 inhibition of neurite outgrowth. DRG neurons treated with dominant negative rac1 remain sensitive to myelin-induced growth cone collapse. Similar mutants of cdc42 do not alter growth cone structure, neurite elongation, or collapsin-1 sensitivity. Whereas the addition of activated rho has no effect, the inhibition of rho with Clostridium botulinum C3 transferase stimulates the outgrowth of DRG neurites. C3 transferase-treated growth cones exhibit little or no lamellipodial spreading and are minimally responsive to collapsin-1 and myelin. These data demonstrate a prominent role for rho and rac1 in modulating growth cone motility and indicate that rac1 may mediate collapsin-1 action.
Key words: collapsin-1; semaphorin; rac1; rho; growth cone collapse; neurite outgrowth; dorsal root ganglion neuron
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Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites
J. Neurosci., December 1, 1997; 17(23): 9183 - 9193.
[Abstract] [Full Text] [PDF]
Y. Gu and Y. Ihara
Evidence That Collapsin Response Mediator Protein-2 Is Involved in the Dynamics of Microtubules
J. Biol. Chem., June 9, 2000; 275(24): 17917 - 17920.
[Abstract] [Full Text] [PDF]
N. Arimura, N. Inagaki, K. Chihara, C. Menager, N. Nakamura, M. Amano, A. Iwamatsu, Y. Goshima, and K. Kaibuchi
Phosphorylation of Collapsin Response Mediator Protein-2 by Rho-kinase. EVIDENCE FOR TWO SEPARATE SIGNALING PATHWAYS FOR GROWTH CONE COLLAPSE
J. Biol. Chem., July 28, 2000; 275(31): 23973 - 23980.
[Abstract] [Full Text] [PDF]
G. B. Whitaker, B. J. Limberg, and J. S. Rosenbaum
Vascular Endothelial Growth Factor Receptor-2 and Neuropilin-1 Form a Receptor Complex That Is Responsible for the Differential Signaling Potency of VEGF165 and VEGF121
J. Biol. Chem., June 29, 2001; 276(27): 25520 - 25531.
[Abstract] [Full Text] [PDF]
H. G. Vikis, W. Li, Z. He, and K.-L. Guan
The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner
PNAS, November 7, 2000; 97(23): 12457 - 12462.
[Abstract] [Full Text] [PDF]
B. J. Eickholt, F. S. Walsh, and P. Doherty
An inactive pool of GSK-3 at the leading edge of growth cones is implicated in Semaphorin 3A signaling
J. Cell Biol., April 15, 2002; 157(2): 211 - 217.
[Abstract] [Full Text] [PDF]
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