The extracellular domain of the TGFβ type II receptor regulates membrane raft partitioning

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DOIResolve DOI: http://doi.org/10.1042/BJ20081131
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TypeArticle
Journal titleBiochemical Journal
Volume421
Issue1
Pages119131; # of pages: 13
Subjectgranulocyte/macrophage colony-stimulating factor (GMCSF); mannosyl(α-1,6)-glycoprotein β-1,6-N-acetylglucosaminyltransferase V (Mgat5); transforming growth factor β (TGFβ); transforming growth factor β type II receptor (TβRII)
AbstractCell-surface TGFβ (transforming growth factor β) receptors partition into membrane rafts and the caveolin-positive endocytic compartment by an unknown mechanism. In the present study, we investigated the determinant in the TGFβ type II receptor (TβRII) that is necessary for membrane raft/caveolar targeting. Using subcellular fractionation and immunofluorescence microscopy techniques, we demonstrated that the extracellular domain of TβRII mediates receptor partitioning into raft and caveolin-positive membrane domains. Pharmacological perturbation of glycosylation using tunicamycin or the mutation of Mgat5 [mannosyl(α-1,6)-glycoprotein β-1,6-N-acetylglucosaminyltransferase V] activity interfered with the raft partitioning of TβRII. However, this was not due to the glycosylation state of TβRII, as a non-glycosylated TβRII mutant remained enriched in membrane rafts. This suggested that other cell-surface glycoproteins associate with the extracellular domain of TβRII and direct their partitioning in membrane raft domains. To test this we analysed a GMCSF (granulocyte/macrophage colony-stimulating factor)–TβRII chimaeric receptor, which contains a glycosylated GMCSF extracellular domain fused to the transmembrane and intracellular domains of TβRII. This chimaeric receptor was found to be largely excluded from membrane rafts and caveolin-positive structures. Our results indicate that the extracellular domain of TβRII mediates receptor partitioning into membrane rafts and efficient entrance into caveolin-positive endosomes.
Publication date
PublisherPortland Press
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedYes
NRC number53197
NPARC number21268265
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Record identifiercdad4fca-05d9-4f35-9dc7-10db2bb46621
Record created2013-06-11
Record modified2016-05-09
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