Hydrophobic‐Domain‐Dependent Protein–Protein Interactions Mediate the Localization of GPAT Enzymes to ER Subdomains
The endoplasmic reticulum (ER) is a dynamic organelle that consists of numerous regions or ‘subdomains’ that have discrete morphological features and functional properties. Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear underst...
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description | The endoplasmic reticulum (ER) is a dynamic organelle that consists of numerous regions or ‘subdomains’ that have discrete morphological features and functional properties. Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear understanding of how they are assembled and maintained has not been well established. We previously demonstrated that two diacylglycerol acyltransferase enzymes (DGAT1 and DGAT2) from tung tree (Vernicia fordii) were located in different subdomains of ER, but the mechanisms responsible for protein targeting to these subdomains were not elucidated. Here we extend these studies by describing two glycerol‐3‐phosphate acyltransferase‐like (GPAT) enzymes from tung tree, GPAT8 and GPAT9, that both colocalize with DGAT2 in the same ER subdomains. Measurement of protein–protein interactions using the split‐ubiquitin assay revealed that GPAT8 interacts with itself, GPAT9 and DGAT2, but not with DGAT1. Furthermore, mutational analysis of GPAT8 revealed that the protein's first predicted hydrophobic region, which contains an amphipathic helix‐like motif, is required for interaction with DGAT2 and for DGAT2‐dependent colocalization in ER subdomains. Taken together, these results suggest that the regulation and organization of ER subdomains is mediated at least in part by higher‐ordered, hydrophobic‐domain‐dependent homo‐ and hetero‐oligomeric protein–protein interactions. |
doi_str_mv | 10.1111/j.1600-0854.2011.01160.x |
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Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear understanding of how they are assembled and maintained has not been well established. We previously demonstrated that two diacylglycerol acyltransferase enzymes (DGAT1 and DGAT2) from tung tree (Vernicia fordii) were located in different subdomains of ER, but the mechanisms responsible for protein targeting to these subdomains were not elucidated. Here we extend these studies by describing two glycerol‐3‐phosphate acyltransferase‐like (GPAT) enzymes from tung tree, GPAT8 and GPAT9, that both colocalize with DGAT2 in the same ER subdomains. Measurement of protein–protein interactions using the split‐ubiquitin assay revealed that GPAT8 interacts with itself, GPAT9 and DGAT2, but not with DGAT1. Furthermore, mutational analysis of GPAT8 revealed that the protein's first predicted hydrophobic region, which contains an amphipathic helix‐like motif, is required for interaction with DGAT2 and for DGAT2‐dependent colocalization in ER subdomains. 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Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear understanding of how they are assembled and maintained has not been well established. We previously demonstrated that two diacylglycerol acyltransferase enzymes (DGAT1 and DGAT2) from tung tree (Vernicia fordii) were located in different subdomains of ER, but the mechanisms responsible for protein targeting to these subdomains were not elucidated. Here we extend these studies by describing two glycerol‐3‐phosphate acyltransferase‐like (GPAT) enzymes from tung tree, GPAT8 and GPAT9, that both colocalize with DGAT2 in the same ER subdomains. Measurement of protein–protein interactions using the split‐ubiquitin assay revealed that GPAT8 interacts with itself, GPAT9 and DGAT2, but not with DGAT1. Furthermore, mutational analysis of GPAT8 revealed that the protein's first predicted hydrophobic region, which contains an amphipathic helix‐like motif, is required for interaction with DGAT2 and for DGAT2‐dependent colocalization in ER subdomains. Taken together, these results suggest that the regulation and organization of ER subdomains is mediated at least in part by higher‐ordered, hydrophobic‐domain‐dependent homo‐ and hetero‐oligomeric protein–protein interactions.</description><subject>Aleurites - enzymology</subject><subject>Aleurites - genetics</subject><subject>Aleurites - metabolism</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Cells, Cultured</subject><subject>diacylglycerol acyltransferase</subject><subject>Diacylglycerol O-Acyltransferase - chemistry</subject><subject>Diacylglycerol O-Acyltransferase - metabolism</subject><subject>endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - enzymology</subject><subject>Glycerol-3-Phosphate O-Acyltransferase - chemistry</subject><subject>Glycerol-3-Phosphate O-Acyltransferase - genetics</subject><subject>Glycerol-3-Phosphate O-Acyltransferase - metabolism</subject><subject>glycerol‐3‐phosphate acyltransferase</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Structure, Tertiary</subject><subject>protein targeting</subject><subject>protein topology</subject><subject>Protein Transport</subject><subject>protein–protein interactions</subject><subject>subdomain</subject><subject>Yeasts</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1OwzAMxyME4mPwCig3Ti1Om7bpgcME40MaAsHuUZK6olPbjKYTKyceAYk35Elot8EZS5b_sv-2pR8hlIHP-jif-ywG8EBE3A-AMb_PGPzVDjn8G-z2OkyFlwYsPSBHzs0BIIg43ycHAQsYTwAOSXfbZY1dvFhdmO-PzytbqaIeBC6wzrBu6WNjWxx6X1tF7-oWG2XawtaO3mNWqBZp-4J0ao0qi3c1TKjN6c3jeEYn9XtXoaOtpZMn-rzU2fqHOyZ7uSodnmzriMyuJ7PLW2_6cHN3OZ56hgsOXpgyzU2iIx4FhmdpjjrLGQ8hi3nMVZiGoFkeCxOrIEGBuU5ygaHWLDUMVDgiZ5uzi8a-LtG1siqcwbJUNdqlkyISiQCRRr1TbJymsc41mMtFU1Sq6SQDOWCXcznQlQNdOWCXa-xy1a-ebp8sdYXZ3-Iv595wsTG8FSV2_z4sZ0_jQYU_OiWVKw</recordid><startdate>201104</startdate><enddate>201104</enddate><creator>Gidda, Satinder K.</creator><creator>Shockey, Jay M.</creator><creator>Falcone, Mina</creator><creator>Kim, Peter K.</creator><creator>Rothstein, Steven J.</creator><creator>Andrews, David W.</creator><creator>Dyer, John M.</creator><creator>Mullen, Robert T.</creator><general>Blackwell Publishing Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201104</creationdate><title>Hydrophobic‐Domain‐Dependent Protein–Protein Interactions Mediate the Localization of GPAT Enzymes to ER Subdomains</title><author>Gidda, Satinder K. ; 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Although it is generally accepted that these subdomains differ in their protein and perhaps lipid compositions, a clear understanding of how they are assembled and maintained has not been well established. We previously demonstrated that two diacylglycerol acyltransferase enzymes (DGAT1 and DGAT2) from tung tree (Vernicia fordii) were located in different subdomains of ER, but the mechanisms responsible for protein targeting to these subdomains were not elucidated. Here we extend these studies by describing two glycerol‐3‐phosphate acyltransferase‐like (GPAT) enzymes from tung tree, GPAT8 and GPAT9, that both colocalize with DGAT2 in the same ER subdomains. Measurement of protein–protein interactions using the split‐ubiquitin assay revealed that GPAT8 interacts with itself, GPAT9 and DGAT2, but not with DGAT1. Furthermore, mutational analysis of GPAT8 revealed that the protein's first predicted hydrophobic region, which contains an amphipathic helix‐like motif, is required for interaction with DGAT2 and for DGAT2‐dependent colocalization in ER subdomains. Taken together, these results suggest that the regulation and organization of ER subdomains is mediated at least in part by higher‐ordered, hydrophobic‐domain‐dependent homo‐ and hetero‐oligomeric protein–protein interactions.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>21214700</pmid><doi>10.1111/j.1600-0854.2011.01160.x</doi><tpages>21</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Aleurites - enzymology Aleurites - genetics Aleurites - metabolism Amino Acid Motifs Amino Acid Sequence Cells, Cultured diacylglycerol acyltransferase Diacylglycerol O-Acyltransferase - chemistry Diacylglycerol O-Acyltransferase - metabolism endoplasmic reticulum Endoplasmic Reticulum - enzymology Glycerol-3-Phosphate O-Acyltransferase - chemistry Glycerol-3-Phosphate O-Acyltransferase - genetics Glycerol-3-Phosphate O-Acyltransferase - metabolism glycerol‐3‐phosphate acyltransferase Membrane Proteins - chemistry Membrane Proteins - metabolism Molecular Sequence Data Protein Interaction Domains and Motifs Protein Structure, Tertiary protein targeting protein topology Protein Transport protein–protein interactions subdomain Yeasts |
title | Hydrophobic‐Domain‐Dependent Protein–Protein Interactions Mediate the Localization of GPAT Enzymes to ER Subdomains |
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