QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fang, X. Articles by Stallcup, W. B. Search for Related Content PubMed PubMed Citation Articles by Fang, X. Articles by Stallcup, W. B.

Vol. 10, Issue 10, 3373-3387, October 1999

Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

Xuexun Fang, Michael A. Burg,^* Diana Barritt, Kimberlee Dahlin-Huppe, Akiko Nishiyama, and William B. Stallcup

The Burnham Institute, La Jolla Cancer Research Center, La Jolla, California 92037

Cells expressing the NG2 proteoglycan can attach, spread, and migrate on surfaces coated with NG2 mAbs, demonstrating that engagement of NG2 can trigger the cytoskeletal rearrangements necessary for changes in cell morphology and motility. Engagement of different epitopes of the proteoglycan results in distinct forms of actin reorganization. On mAb D120, the cells contain radial actin spikes characteristic of filopodial extension, whereas on mAb N143, the cells contain cortical actin bundles characteristic of lamellipodia. Cells that express NG2 variants lacking the transmembrane and cytoplasmic domains are unable to spread or migrate on NG2 mAb-coated surfaces, indicating that these portions of the molecule are essential for NG2-mediated signal transduction. Cells expressing an NG2 variant lacking the C-terminal half of the cytoplasmic domain can still spread normally on mAbs D120 and N143, suggesting that the membrane-proximal cytoplasmic segment is responsible for this process. In contrast, this variant migrates poorly on mAb D120 and exhibits abnormal arrays of radial actin filaments decorated with fascin during spreading on this mAb. The C-terminal portion of the NG2 cytoplasmic domain, therefore, may be involved in regulating molecular events that are crucial for cell motility.

---

   Present addresses: ^*Selective Genetics, 11035 Roselle Street, San Diego, CA 92121; Department of Physiology and Neurobiology, University of Connecticut, 3107 Horsebarn Hill Road, U-156, Storrs, CT 06269-4156.
   Corresponding author. E-mail address: stallcup{at}burnham-inst.org.

---

Molecular Biology of the Cell
Vol. 10, 3373-3387, October 1999
Copyright © 1999 by The American Society for Cell Biology

This article has been cited by other articles:

				I. T. Makagiansar, S. Williams, T. Mustelin, and W. B. Stallcup Differential phosphorylation of NG2 proteoglycan by ERK and PKC{alpha} helps balance cell proliferation and migration J. Cell Biol., October 3, 2007; 178(1): 155 - 165. [Abstract] [Full Text] [PDF]

				C. Erfurt, Z. Sun, I. Haendle, B. Schuler-Thurner, C. Heirman, K. Thielemans, P. van der Bruggen, G. Schuler, and E. S. Schultz Tumor-Reactive CD4+ T Cell Responses to the Melanoma-Associated Chondroitin Sulphate Proteoglycan in Melanoma Patients and Healthy Individuals in the Absence of Autoimmunity J. Immunol., June 15, 2007; 178(12): 7703 - 7709. [Abstract] [Full Text] [PDF]

				W. Luo, E. Ko, J. C.-f. Hsu, X. Wang, and S. Ferrone Targeting Melanoma Cells with Human High Molecular Weight-Melanoma Associated Antigen-Specific Antibodies Elicited by a Peptide Mimotope: Functional Effects J. Immunol., May 15, 2006; 176(10): 6046 - 6054. [Abstract] [Full Text] [PDF]

				Y. Li, J. Wang, S. M. A. Rizvi, M. J. Jager, R. M. Conway, F. A. Billson, B. J. Allen, and M. C. Madigan In Vitro Targeting of NG2 Antigen by 213Bi-9.2.27 {alpha}-Immunoconjugate Induces Cytotoxicity in Human Uveal Melanoma Cells Invest. Ophthalmol. Vis. Sci., December 1, 2005; 46(12): 4365 - 4371. [Abstract] [Full Text] [PDF]

				I. T. Makagiansar, S. Williams, K. Dahlin-Huppe, J.-i. Fukushi, T. Mustelin, and W. B. Stallcup Phosphorylation of NG2 Proteoglycan by Protein Kinase C-{alpha} Regulates Polarized Membrane Distribution and Cell Motility J. Biol. Chem., December 31, 2004; 279(53): 55262 - 55270. [Abstract] [Full Text] [PDF]

				I. Smyth, X. Du, M. S. Taylor, M. J. Justice, B. Beutler, and I. J. Jackson The extracellular matrix gene Frem1 is essential for the normal adhesion of the embryonic epidermis PNAS, September 14, 2004; 101(37): 13560 - 13565. [Abstract] [Full Text] [PDF]

				J. Legg, U. B. Jensen, S. Broad, I. Leigh, and F. M. Watt Role of melanoma chondroitin sulphate proteoglycan in patterning stem cells in human interfollicular epidermis Development, December 15, 2003; 130(24): 6049 - 6063. [Abstract] [Full Text] [PDF]

				M. Shigeta, N. Sanzen, M. Ozawa, J. Gu, H. Hasegawa, and K. Sekiguchi CD151 regulates epithelial cell-cell adhesion through PKC- and Cdc42-dependent actin cytoskeletal reorganization J. Cell Biol., October 13, 2003; 163(1): 165 - 176. [Abstract] [Full Text] [PDF]

				W. B. Stallcup and K. Dahlin-Huppe Chondroitin sulfate and cytoplasmic domain-dependent membrane targeting of the NG2 proteoglycan promotes retraction fiber formation and cell polarization J. Cell Sci., March 8, 2002; 114(12): 2315 - 2325. [Abstract] [Full Text] [PDF]

				S. Schneider, F. Bosse, D. D'Urso, H.-W. Muller, M. W. Sereda, K.-A. Nave, A. Niehaus, T. Kempf, M. Schnolzer, and J. Trotter The AN2 Protein Is a Novel Marker for the Schwann Cell Lineage Expressed by Immature and Nonmyelinating Schwann Cells J. Neurosci., February 1, 2001; 21(3): 920 - 933. [Abstract] [Full Text] [PDF]

				L. Goretzki, C. R. Lombardo, and W. B. Stallcup Binding of the NG2 Proteoglycan to Kringle Domains Modulates the Functional Properties of Angiostatin and Plasmin(ogen) J. Biol. Chem., September 8, 2000; 275(37): 28625 - 28633. [Abstract] [Full Text] [PDF]