View in EDS

Drosophila Heparan Sulfate 6-O-Endosulfatase Sulf1 Facilitates Wingless (Wg) Protein Degradation.

Saved in:
Bibliographic Details
Title: Drosophila Heparan Sulfate 6-O-Endosulfatase Sulf1 Facilitates Wingless (Wg) Protein Degradation.
Authors: Kleinschmit, Adam1, Takemura, Masahiko1, Dejima, Katsufumi1, Pui Yee Choi1, Nakato, Hiroshi1 nakat003@umn.edu
Source: Journal of Biological Chemistry. 2/15/2013, Vol. 288 Issue 7, p5081-5089. 9p.
Subjects: Heparan sulfate proteoglycans, Heparan sulfate, Sulfotransferases, Golgi apparatus, Proteoglycans, Drosophila, Sulfates
Abstract: Heparan sulfate proteoglycans regulate various physiological and developmental processes through interactions with a number of protein ligands. Heparan sulfate (HS)-ligand binding depends on the amount and patterns of sulfate groups on HS, which are controlled by various HS sulfotransferases in the Golgi apparatus as well as extracellular 6-O-endosulfatases called "Sulfs." Sulfs are a family of secreted molecules that specifically remove 6-O-sulfate groups within the highly sulfated regions on HS. Vertebrate Sulfs promote Wnt signaling, whereas the only Drosophila homologue of Sulfs, Sulf1, negatively regulates Wingless (Wg) signaling. To understand the molecular mechanism for the negative regulation of Wg signaling by Sulf1, we studied the effects of Sulf1 on HS-Wg interaction and Wg stability. Sulf1 overexpression strongly inhibited the binding of Wg to Dally, a potential target heparan sulfate proteoglycan of Sulf1. This effect of Drosophila Sulf1 on the HS-Wg interaction is similar to that of vertebrate Sulfs. Using in vitro, in vivo, and ex vivo systems, we show that Sulf1 reduces extracellularWgprotein levels, at least partly by facilitatingWg degradation. In addition, expression of human Sulf1 in the Drosophila wing disc lowers the levels of extracellular Wg protein, as observed for Drosophila Sulf1. Our study demonstrates that vertebrate and Drosophila Sulfs have an intrinsically similar activity and that the function of Sulfs in the fate of Wnt/Wg ligands is context-dependent. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 85849408
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Drosophila Heparan Sulfate 6-O-Endosulfatase Sulf1 Facilitates Wingless (Wg) Protein Degradation.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Kleinschmit%2C+Adam%22">Kleinschmit, Adam</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Takemura%2C+Masahiko%22">Takemura, Masahiko</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Dejima%2C+Katsufumi%22">Dejima, Katsufumi</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Pui+Yee+Choi%22">Pui Yee Choi</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Nakato%2C+Hiroshi%22">Nakato, Hiroshi</searchLink><relatesTo>1</relatesTo><i> nakat003@umn.edu</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 2/15/2013, Vol. 288 Issue 7, p5081-5089. 9p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Heparan+sulfate+proteoglycans%22">Heparan sulfate proteoglycans</searchLink><br /><searchLink fieldCode="DE" term="%22Heparan+sulfate%22">Heparan sulfate</searchLink><br /><searchLink fieldCode="DE" term="%22Sulfotransferases%22">Sulfotransferases</searchLink><br /><searchLink fieldCode="DE" term="%22Golgi+apparatus%22">Golgi apparatus</searchLink><br /><searchLink fieldCode="DE" term="%22Proteoglycans%22">Proteoglycans</searchLink><br /><searchLink fieldCode="DE" term="%22Drosophila%22">Drosophila</searchLink><br /><searchLink fieldCode="DE" term="%22Sulfates%22">Sulfates</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Heparan sulfate proteoglycans regulate various physiological and developmental processes through interactions with a number of protein ligands. Heparan sulfate (HS)-ligand binding depends on the amount and patterns of sulfate groups on HS, which are controlled by various HS sulfotransferases in the Golgi apparatus as well as extracellular 6-O-endosulfatases called "Sulfs." Sulfs are a family of secreted molecules that specifically remove 6-O-sulfate groups within the highly sulfated regions on HS. Vertebrate Sulfs promote Wnt signaling, whereas the only Drosophila homologue of Sulfs, Sulf1, negatively regulates Wingless (Wg) signaling. To understand the molecular mechanism for the negative regulation of Wg signaling by Sulf1, we studied the effects of Sulf1 on HS-Wg interaction and Wg stability. Sulf1 overexpression strongly inhibited the binding of Wg to Dally, a potential target heparan sulfate proteoglycan of Sulf1. This effect of Drosophila Sulf1 on the HS-Wg interaction is similar to that of vertebrate Sulfs. Using in vitro, in vivo, and ex vivo systems, we show that Sulf1 reduces extracellularWgprotein levels, at least partly by facilitatingWg degradation. In addition, expression of human Sulf1 in the Drosophila wing disc lowers the levels of extracellular Wg protein, as observed for Drosophila Sulf1. Our study demonstrates that vertebrate and Drosophila Sulfs have an intrinsically similar activity and that the function of Sulfs in the fate of Wnt/Wg ligands is context-dependent. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=85849408
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1074/jbc.M112.447029
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 9
        StartPage: 5081
    Subjects:
      – SubjectFull: Heparan sulfate proteoglycans
        Type: general
      – SubjectFull: Heparan sulfate
        Type: general
      – SubjectFull: Sulfotransferases
        Type: general
      – SubjectFull: Golgi apparatus
        Type: general
      – SubjectFull: Proteoglycans
        Type: general
      – SubjectFull: Drosophila
        Type: general
      – SubjectFull: Sulfates
        Type: general
    Titles:
      – TitleFull: Drosophila Heparan Sulfate 6-O-Endosulfatase Sulf1 Facilitates Wingless (Wg) Protein Degradation.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Kleinschmit, Adam
      – PersonEntity:
          Name:
            NameFull: Takemura, Masahiko
      – PersonEntity:
          Name:
            NameFull: Dejima, Katsufumi
      – PersonEntity:
          Name:
            NameFull: Pui Yee Choi
      – PersonEntity:
          Name:
            NameFull: Nakato, Hiroshi
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 15
              M: 02
              Text: 2/15/2013
              Type: published
              Y: 2013
          Identifiers:
            – Type: issn-print
              Value: 00219258
          Numbering:
            – Type: volume
              Value: 288
            – Type: issue
              Value: 7
          Titles:
            – TitleFull: Journal of Biological Chemistry
              Type: main
ResultId 1