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Regulation of Notch signaling by Drosophila heparan sulfate 3-O sulfotransferase.


ABSTRACT: Heparan sulfate (HS) regulates the activity of various ligands and is involved in molecular recognition events on the cell surface and in the extracellular matrix. Specific binding of HS to different ligand proteins depends on the sulfation pattern of HS. For example, the interaction between antithrombin and a particular 3-O sulfated HS motif is thought to modulate blood coagulation. However, a recent study of mice defective for this modification suggested that 3-O sulfation plays other biological roles. Here, we show that Drosophila melanogaster HS 3-O sulfotransferase-b (Hs3st-B), which catalyzes HS 3-O sulfation, is a novel component of the Notch pathway. Reduction of Hs3st-B function by transgenic RNA interference compromised Notch signaling, producing neurogenic phenotypes. We also show that levels of Notch protein on the cell surface were markedly decreased by loss of Hs3st-B. These findings suggest that Hs3st-B is involved in Notch signaling by affecting stability or intracellular trafficking of Notch protein.

SUBMITTER: Kamimura K 

PROVIDER: S-EPMC2172002 | biostudies-literature | 2004 Sep

REPOSITORIES: biostudies-literature

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Regulation of Notch signaling by Drosophila heparan sulfate 3-O sulfotransferase.

Kamimura Keisuke K   Rhodes John M JM   Ueda Ryu R   McNeely Melissa M   Shukla Deepak D   Kimata Koji K   Spear Patricia G PG   Shworak Nicholas W NW   Nakato Hiroshi H  

The Journal of cell biology 20040901 7


Heparan sulfate (HS) regulates the activity of various ligands and is involved in molecular recognition events on the cell surface and in the extracellular matrix. Specific binding of HS to different ligand proteins depends on the sulfation pattern of HS. For example, the interaction between antithrombin and a particular 3-O sulfated HS motif is thought to modulate blood coagulation. However, a recent study of mice defective for this modification suggested that 3-O sulfation plays other biologic  ...[more]

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