Glycosyltransferase-specific Golgi-targeting mechanisms.

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  • Author(s): Petrosyan A;Petrosyan A; Ali MF; Cheng PW
  • Source:
    The Journal of biological chemistry [J Biol Chem] 2012 Nov 02; Vol. 287 (45), pp. 37621-7. Date of Electronic Publication: 2012 Sep 17.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Galactosyltransferases/*metabolism ; Golgi Apparatus/*enzymology ; N-Acetylglucosaminyltransferases/*metabolism ; Transport Vesicles/*enzymology; Autoantigens/genetics ; Autoantigens/metabolism ; Blotting, Western ; Cell Line, Tumor ; Coatomer Protein/genetics ; Coatomer Protein/metabolism ; Galactosyltransferases/genetics ; Glycosylation ; Golgi Matrix Proteins ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Microscopy, Confocal ; Microscopy, Fluorescence ; N-Acetylglucosaminyltransferases/genetics ; Protein Binding ; Protein Transport ; RNA Interference ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; Red Fluorescent Protein
    • Abstract:
      Glycosylation of secreted and membrane-bound mucins is carried out by glycosyltransferases localized to specific Golgi compartments according to the step in which each enzyme participates. However, the Golgi-targeting mechanisms of these enzymes are not clear. Herein, we investigate the Golgi-targeting mechanisms of core 1 β3 galactosyltransferase (C1GalT1) and core 2 β1,6-N-acetylglucosaminyltransferase-2 or mucus type (C2GnT-M), which participate in the early O-glycosylation steps. siRNAs, co-immunoprecipitation, and confocal fluorescence microscopy were employed to identify the golgins involved in the Golgi docking of vesicular complexes (VCs) that carry these two enzymes. We have found that these VCs use different golgins for docking: C2GnT-M-carrying VC (C2GnT-M-VC) utilizes Giantin, whereas C1GalT1-VC employs GM130-GRASP65 complex. However, in the absence of GRASP65, C1GalT1-VC utilizes GM130-Giantin complex. Also, we have found that these VCs are 1.1-1.2 μm in diameter, specific for each enzyme, and independent of coat protein complex II and I (COPII and COPI). These two fluorescently tagged enzymes exhibit different fluorescence recovery times in the Golgi after photobleaching. Thus, novel enzyme-specific Golgi-targeting mechanisms are employed by glycosyltransferases, and multiple Golgi docking strategies are utilized by C1GalT1.
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    • Grant Information:
      2R01HL48282 United States HL NHLBI NIH HHS; 1R21HL097238 United States HL NHLBI NIH HHS; I01 BX000985 United States BX BLRD VA; R01 HL048282 United States HL NHLBI NIH HHS; R21 HL097238 United States HL NHLBI NIH HHS
    • Accession Number:
      0 (Autoantigens)
      0 (Coatomer Protein)
      0 (GORASP1 protein, human)
      0 (Golgi Matrix Proteins)
      0 (Golgin subfamily A member 2)
      0 (Luminescent Proteins)
      0 (Membrane Proteins)
      0 (Vesicular Transport Proteins)
      0 (macrogolgin)
      147336-22-9 (Green Fluorescent Proteins)
      EC 2.4.1.- (C1GALT1 protein, human)
      EC 2.4.1.- (Galactosyltransferases)
      EC 2.4.1.- (N-Acetylglucosaminyltransferases)
      EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3)
    • Publication Date:
      Date Created: 20120919 Date Completed: 20130123 Latest Revision: 20231213
    • Publication Date:
      20240829
    • Accession Number:
      PMC3488040
    • Accession Number:
      10.1074/jbc.C112.403006
    • Accession Number:
      22988244