QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend 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 Stallcup, W. B. Articles by Dahlin-Huppe, K. Search for Related Content PubMed PubMed Citation Articles by Stallcup, W. B. Articles by Dahlin-Huppe, K. Social Bookmarking                         What's this?

Chondroitin sulfate and cytoplasmic domain-dependent membrane targeting of the NG2 proteoglycan promotes retraction fiber formation and cell polarization

The Burnham Institute, La Jolla Cancer Research Center, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA

*Author for correspondence (e-mail: stallcup{at}burnham.org)

Accepted March 20, 2001

Targeting of the NG2 proteoglycan to cellular retraction fibers was studied by expressing mutant NG2 molecules lacking specific structural elements of the proteoglycan. Both the cytoplasmic domain and the chondroitin sulfate chain of NG2 appear to have roles in sorting NG2 to subcellular microdomains destined to become retraction fibers. Neither of these structural features alone is sufficient to allow optimal targeting of NG2 to retraction fibers, but together they promote efficient localization of the proteoglycan to these sites. This pattern of NG2 sorting seems to be necessary for optimal retraction fiber formation, as cells expressing poorly targeted NG2 mutants are noticeably deficient in their ability to extend retraction fibers. Furthermore, retraction fiber formation correlates strongly with the tendency of cells to assume a polarized morphology with NG2-positive retraction fibers at one pole of the cell and actin-rich lamellipodia at the other. This polarization can be triggered either through engagement of NG2 by the substratum or by exposure to lysophosphatidic acid, a potent activator of the rho GTPase. These results suggest a possible role for NG2 in regulating rho-dependent mechanisms in the trailing processes of motile cells.

Key words: NG2 proteoglycan, Chondroitin sulfate, Cytoplasmic domain, Membrane sorting, Retraction fibers, Cell polarity

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				Y. M. Ughrin, Z. J. Chen, and J. M. Levine Multiple Regions of the NG2 Proteoglycan Inhibit Neurite Growth and Induce Growth Cone Collapse J. Neurosci., January 1, 2003; 23(1): 175 - 186. [Abstract] [Full Text] [PDF]

				L. L. Jones, Y. Yamaguchi, W. B. Stallcup, and M. H. Tuszynski NG2 Is a Major Chondroitin Sulfate Proteoglycan Produced after Spinal Cord Injury and Is Expressed by Macrophages and Oligodendrocyte Progenitors J. Neurosci., April 1, 2002; 22(7): 2792 - 2803. [Abstract] [Full Text] [PDF]