Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface
Caveolar endocytosis has an important function in the cellular uptake of some bacterial toxins, viruses and circulating proteins. However, the molecular machinery involved in regulating caveolar uptake is poorly defined. Here, we demonstrate that caveolar endocytosis is regulated by syntaxin 6, a ta...
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| Veröffentlicht in: | Nature cell biology 2006-04, Vol.8 (4), p.317-328 |
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| creator | Choudhury, Amit Marks, David L. Proctor, Kirsty M. Gould, Gwyn W. Pagano, Richard E. |
| description | Caveolar endocytosis has an important function in the cellular uptake of some bacterial toxins, viruses and circulating proteins. However, the molecular machinery involved in regulating caveolar uptake is poorly defined. Here, we demonstrate that caveolar endocytosis is regulated by syntaxin 6, a target membrane soluble N-ethylmaleimide attachment protein receptor (t-SNARE) involved in membrane fusion events along the secretory pathway. When syntaxin 6 function was inhibited, internalization through caveolae was dramatically reduced, whereas other endocytic mechanisms were unaffected. Syntaxin 6 inhibition also reduced the presence of caveolin-1 and caveolae at the plasma membrane. In addition, syntaxin 6 inhibition decreased the delivery of GM1 ganglioside (GM1) and glycosylphosphatidylinositol (GPI)–GFP (but not vesicular stomatitis virus-glycoprotein G; VSV-G) protein from the Golgi complex to the plasma membrane. Addition of GM1 to syntaxin 6-inhibited cells resulted in the reappearance of caveolin-1 and caveolae at the plasma membrane, and restored caveolar uptake. These results suggest that syntaxin 6 regulates the delivery of microdomain-associated lipids and proteins to the cell surface, which are required for caveolar endocytosis. |
| doi_str_mv | 10.1038/ncb1380 |
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However, the molecular machinery involved in regulating caveolar uptake is poorly defined. Here, we demonstrate that caveolar endocytosis is regulated by syntaxin 6, a target membrane soluble N-ethylmaleimide attachment protein receptor (t-SNARE) involved in membrane fusion events along the secretory pathway. When syntaxin 6 function was inhibited, internalization through caveolae was dramatically reduced, whereas other endocytic mechanisms were unaffected. Syntaxin 6 inhibition also reduced the presence of caveolin-1 and caveolae at the plasma membrane. In addition, syntaxin 6 inhibition decreased the delivery of GM1 ganglioside (GM1) and glycosylphosphatidylinositol (GPI)–GFP (but not vesicular stomatitis virus-glycoprotein G; VSV-G) protein from the Golgi complex to the plasma membrane. Addition of GM1 to syntaxin 6-inhibited cells resulted in the reappearance of caveolin-1 and caveolae at the plasma membrane, and restored caveolar uptake. These results suggest that syntaxin 6 regulates the delivery of microdomain-associated lipids and proteins to the cell surface, which are required for caveolar endocytosis.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Caveolae</subject><subject>Caveolae - metabolism</subject><subject>Caveolin 1 - metabolism</subject><subject>Cell Biology</subject><subject>Cell Membrane - metabolism</subject><subject>Cell membranes</subject><subject>Cells, Cultured</subject><subject>Cholesterol</subject><subject>Developmental Biology</subject><subject>Endocytosis</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - metabolism</subject><subject>G(M1) Ganglioside - metabolism</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>Golgi Apparatus</subject><subject>Humans</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Lipids</subject><subject>Membrane Glycoproteins - 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Academic</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choudhury, Amit</au><au>Marks, David L.</au><au>Proctor, Kirsty M.</au><au>Gould, Gwyn W.</au><au>Pagano, Richard E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>8</volume><issue>4</issue><spage>317</spage><epage>328</epage><pages>317-328</pages><issn>1465-7392</issn><issn>1476-4679</issn><eissn>1476-4679</eissn><abstract>Caveolar endocytosis has an important function in the cellular uptake of some bacterial toxins, viruses and circulating proteins. However, the molecular machinery involved in regulating caveolar uptake is poorly defined. Here, we demonstrate that caveolar endocytosis is regulated by syntaxin 6, a target membrane soluble N-ethylmaleimide attachment protein receptor (t-SNARE) involved in membrane fusion events along the secretory pathway. When syntaxin 6 function was inhibited, internalization through caveolae was dramatically reduced, whereas other endocytic mechanisms were unaffected. Syntaxin 6 inhibition also reduced the presence of caveolin-1 and caveolae at the plasma membrane. In addition, syntaxin 6 inhibition decreased the delivery of GM1 ganglioside (GM1) and glycosylphosphatidylinositol (GPI)–GFP (but not vesicular stomatitis virus-glycoprotein G; VSV-G) protein from the Golgi complex to the plasma membrane. Addition of GM1 to syntaxin 6-inhibited cells resulted in the reappearance of caveolin-1 and caveolae at the plasma membrane, and restored caveolar uptake. These results suggest that syntaxin 6 regulates the delivery of microdomain-associated lipids and proteins to the cell surface, which are required for caveolar endocytosis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>16565709</pmid><doi>10.1038/ncb1380</doi><tpages>12</tpages></addata></record> |
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| subjects | Biochemistry Biomedical and Life Sciences Cancer Research Caveolae Caveolae - metabolism Caveolin 1 - metabolism Cell Biology Cell Membrane - metabolism Cell membranes Cells, Cultured Cholesterol Developmental Biology Endocytosis Fibroblasts - cytology Fibroblasts - metabolism G(M1) Ganglioside - metabolism Glycosylphosphatidylinositols - metabolism Golgi Apparatus Humans Kinases Life Sciences Lipids Membrane Glycoproteins - metabolism Membranes Molecular biology Oligonucleotides - pharmacology Physiological aspects Plasma Protein Transport Proteins Qa-SNARE Proteins - antagonists & inhibitors Qa-SNARE Proteins - genetics Qa-SNARE Proteins - metabolism Stem Cells Stem Cells - cytology Stem Cells - metabolism Toxins Viral Envelope Proteins - metabolism |
| title | Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface |
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