|
Originally published In Press as doi:10.1074/jbc.M304928200 on July 10, 2003
J. Biol. Chem., Vol. 278, Issue 41, 40282-40295, October 10, 2003
Golgi Localization of Carbohydrate Sulfotransferases Is a Determinant of L-selectin Ligand Biosynthesis*
Christopher L. de Graffenried and
Carolyn R. Bertozzi ¶ || **
From the
Departments of Chemistry and ¶Molecular and Cell Biology and the ||Howard Hughes Medical Institute, University of California, Berkeley, California 94720
Sulfation of endothelial glycoproteins by the sulfotransferase GlcNAc6ST-2 is a regulatory modification that promotes binding of the leukocyte adhesion molecule L-selectin. GlcNAc6ST-2 is a member of a family of related enzymes that act on similar carbohydrate substrates in vitro but discrete glycoproteins in vivo. We demonstrate that GlcNAc6ST-1, -2, and -3 have distinct Golgi distributions, with GlcNAc6ST-1 confined to the trans-Golgi network, GlcNAc6ST-3 confined to the early secretory pathway, and GlcNAc6ST-2 distributed throughout the Golgi. Their localization was correlated with preferred activity on either N-linked or O-linked glycoproteins. A chimera comprising the localization domain of GlcNAc6ST-1 fused to the catalytic domain of GlcNAc6ST-2 was confined to the trans-Golgi network and adopted the substrate preference of GlcNAc6ST-1. We propose a model in which Golgi enzyme localization and competition orchestrate the biosynthesis of L-selectin ligands.
Received for publication, May 12, 2003
, and in revised form, July 8, 2003.
This paper is dedicated to the memory of Frank Rusnak and to Jerry Mohrig on the occasion of his retirement.
* This research was supported in part by National Institutes of Health Grant GM59907. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Supported by a National Science Foundation predoctoral fellowship.
** To whom correspondence should be addressed: Dept. of Chemistry, University of California, Berkeley, Berkeley, CA 94720. Tel.: 510-643-1682; Fax: 510-643-2628; E-mail: bertozzi{at}cchem.berkeley.edu.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
J. Holgersson and J. Lofling
Glycosyltransferases involved in type 1 chain and Lewis antigen biosynthesis exhibit glycan and core chain specificity
Glycobiology,
July 1, 2006;
16(7):
584 - 593.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. L. Tjew, K. L. Brown, R. Kannagi, and P. Johnson
Expression of N-acetylglucosamine 6-O-sulfotransferases (GlcNAc6STs)-1 and -4 in human monocytes: GlcNAc6ST-1 is implicated in the generation of the 6-sulfo N-acetyllactosamine/Lewis x epitope on CD44 and is induced by TNF-{alpha}
Glycobiology,
July 1, 2005;
15(7):
7C - 13C.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. L. de Graffenried, S. T. Laughlin, J. J. Kohler, and C. R. Bertozzi
From the Cover: A small-molecule switch for Golgi sulfotransferases
PNAS,
November 30, 2004;
101(48):
16715 - 16720.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. L. de Graffenried and C. R. Bertozzi
The Stem Region of the Sulfotransferase GlcNAc6ST-1 Is a Determinant of Substrate Specificity
J. Biol. Chem.,
September 17, 2004;
279(38):
40035 - 40043.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
K. Uchimura, K. Kadomatsu, F. M. El-Fasakhany, M. S. Singer, M. Izawa, R. Kannagi, N. Takeda, S. D. Rosen, and T. Muramatsu
N-Acetylglucosamine 6-O-Sulfotransferase-1 Regulates Expression of L-Selectin Ligands and Lymphocyte Homing
J. Biol. Chem.,
August 13, 2004;
279(33):
35001 - 35008.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. Bistrup, D. Tsay, P. Shenoy, M. S. Singer, N. Bangia, S. A. Luther, J. G. Cyster, N. H. Ruddle, and S. D. Rosen
Detection of a Sulfotransferase (HEC-GlcNAc6ST) in High Endothelial Venules of Lymph Nodes and in High Endothelial Venule-Like Vessels within Ectopic Lymphoid Aggregates: Relationship to the MECA-79 Epitope
Am. J. Pathol.,
May 1, 2004;
164(5):
1635 - 1644.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
E. V. Chandrasekaran, S. S. Lakhaman, R. Chawda, C. F. Piskorz, S. Neelamegham, and K. L. Matta
Identification of Physiologically Relevant Substrates for Cloned Gal: 3-O-Sulfotransferases (Gal3STs): DISTINCT HIGH AFFINITY OF Gal3ST-2 and LS180 SULFOTRANSFERASE FOR THE GLOBO H BACKBONE, Gal3ST-3 FOR N-GLYCAN MULTITERMINAL Gal{beta}1,4GlcNAc{beta} UNITS AND 6-SULFOGal{beta}1,4GlcNAc{beta}, AND Gal3ST-4 FOR THE MUCIN CORE-2 TRISACCHARIDE
J. Biol. Chem.,
March 12, 2004;
279(11):
10032 - 10041.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|