Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics
The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize t...
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| Veröffentlicht in: | Molecular biology of the cell 2000-08, Vol.11 (8), p.2719-2731 |
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| container_title | Molecular biology of the cell |
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| creator | Steegmaier, M Oorschot, V Klumperman, J Scheller, R H |
| description | The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells. |
| doi_str_mv | 10.1091/mbc.11.8.2719 |
| format | Article |
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To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. 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Oorschot, V ; Klumperman, J ; Scheller, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-c45c044d7bf71cdf534a159a82b8490666e8347e8046a7bdd32c00b04b6a59ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adrenal Cortex - cytology</topic><topic>Adrenal Cortex - metabolism</topic><topic>Adrenal Cortex - ultrastructure</topic><topic>Animals</topic><topic>Carrier Proteins - metabolism</topic><topic>Endoplasmic Reticulum, Smooth - chemistry</topic><topic>Endoplasmic Reticulum, Smooth - metabolism</topic><topic>Endoplasmic Reticulum, Smooth - ultrastructure</topic><topic>Immediate-Early Proteins</topic><topic>Leydig Cells - cytology</topic><topic>Leydig Cells - metabolism</topic><topic>Macromolecular Substances</topic><topic>Male</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Proteins - physiology</topic><topic>Membrane Proteins - ultrastructure</topic><topic>Munc18 Proteins</topic><topic>Protein Structure, Tertiary</topic><topic>Qa-SNARE Proteins</topic><topic>Qc-SNARE Proteins</topic><topic>R-SNARE Proteins</topic><topic>Rats</topic><topic>Sequence Deletion</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steegmaier, M</creatorcontrib><creatorcontrib>Oorschot, V</creatorcontrib><creatorcontrib>Klumperman, J</creatorcontrib><creatorcontrib>Scheller, R H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Steegmaier, M</au><au>Oorschot, V</au><au>Klumperman, J</au><au>Scheller, R H</au><au>Schekman, Randy W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>11</volume><issue>8</issue><spage>2719</spage><epage>2731</epage><pages>2719-2731</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. 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| subjects | Adrenal Cortex - cytology Adrenal Cortex - metabolism Adrenal Cortex - ultrastructure Animals Carrier Proteins - metabolism Endoplasmic Reticulum, Smooth - chemistry Endoplasmic Reticulum, Smooth - metabolism Endoplasmic Reticulum, Smooth - ultrastructure Immediate-Early Proteins Leydig Cells - cytology Leydig Cells - metabolism Macromolecular Substances Male Membrane Proteins - metabolism Membrane Proteins - physiology Membrane Proteins - ultrastructure Munc18 Proteins Protein Structure, Tertiary Qa-SNARE Proteins Qc-SNARE Proteins R-SNARE Proteins Rats Sequence Deletion Transfection Tumor Cells, Cultured Vesicular Transport Proteins |
| title | Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth endoplasmic reticulum membrane dynamics |
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