Role of the HIV-1 envelope transmembrane domain in intracellular sorting
The envelope protein of lentiviruses are type I transmembrane proteins, and their transmembrane domain contains conserved potentially charged residues. This highly unusual feature would be expected to cause endoplasmic reticulum (ER) localization. The aim of this study was to determine by which mean...
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| Veröffentlicht in: | BMC cell biology 2018-03, Vol.19 (1), p.3-3, Article 3 |
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| creator | Perrin, Jackie Bary, Aurélie Vernay, Alexandre Cosson, Pierre |
| description | The envelope protein of lentiviruses are type I transmembrane proteins, and their transmembrane domain contains conserved potentially charged residues. This highly unusual feature would be expected to cause endoplasmic reticulum (ER) localization. The aim of this study was to determine by which means the HIV-1 Env protein is transported to the cell surface although its transmembrane domain contains a conserved arginine residue.
We expressed various chimeric proteins and analyzed the influence of their transmembrane domain on their intracellular localization. The transmembrane domain of the HIV-1 Env protein does not cause ER retention. This is not due to the presence of conserved glycine residues, or to the position of the arginine residue, but to the length of the transmembrane domain. A shortened version of the Env transmembrane domain causes arginine-dependent ER targeting. Remarkably, the transmembrane domain of the HIV-1 Env protein, although it does not confer ER retention, interacts efficiently with negatively charged residues in the membrane.
These results suggest that the intrinsic properties of the HIV-1 Env transmembrane domain allow the protein to escape ER-retention mechanisms, while maintaining its ability to interact with cellular proteins and to influence cellular physiology. |
| doi_str_mv | 10.1186/s12860-018-0153-4 |
| format | Article |
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We expressed various chimeric proteins and analyzed the influence of their transmembrane domain on their intracellular localization. The transmembrane domain of the HIV-1 Env protein does not cause ER retention. This is not due to the presence of conserved glycine residues, or to the position of the arginine residue, but to the length of the transmembrane domain. A shortened version of the Env transmembrane domain causes arginine-dependent ER targeting. Remarkably, the transmembrane domain of the HIV-1 Env protein, although it does not confer ER retention, interacts efficiently with negatively charged residues in the membrane.
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We expressed various chimeric proteins and analyzed the influence of their transmembrane domain on their intracellular localization. The transmembrane domain of the HIV-1 Env protein does not cause ER retention. This is not due to the presence of conserved glycine residues, or to the position of the arginine residue, but to the length of the transmembrane domain. A shortened version of the Env transmembrane domain causes arginine-dependent ER targeting. Remarkably, the transmembrane domain of the HIV-1 Env protein, although it does not confer ER retention, interacts efficiently with negatively charged residues in the membrane.
These results suggest that the intrinsic properties of the HIV-1 Env transmembrane domain allow the protein to escape ER-retention mechanisms, while maintaining its ability to interact with cellular proteins and to influence cellular physiology.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - metabolism</subject><subject>Arginine</subject><subject>Causes of</subject><subject>Cell Membrane</subject><subject>Cellular proteins</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>env Gene Products, Human Immunodeficiency Virus - chemistry</subject><subject>env Gene Products, Human Immunodeficiency Virus - metabolism</subject><subject>HeLa Cells</subject><subject>HIV (Viruses)</subject><subject>HIV-1 - metabolism</subject><subject>Humans</subject><subject>Intracellular Space - metabolism</subject><subject>Lentivirus</subject><subject>Lentivirus - metabolism</subject><subject>Membrane proteins</subject><subject>Physiological aspects</subject><subject>Protein Domains</subject><subject>Protein Transport</subject><subject>Structure-Activity Relationship</subject><issn>1471-2121</issn><issn>1471-2121</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUVFLwzAQDqLonP4AX6Tgiy_VXJqk3YswRJ0wEER9DWl6mZG2mU0n-O9N3ZQJJjku5L7vch8fISdALwAKeRmAFZKmFIoYIkv5DhkBzyFlwGB3635ADkN4oxTyAug-OWATweOiIzJ79DUm3ib9Kyaz-5cUEmw_sPZLTPpOt6HBpowZk8o32rXJ94kVg3W9qnWXBN_1rl0ckT2r64DHmzwmz7c3T9ezdP5wd389nadGZKxPywmztiilnVhNmRzGsKbiFNHkzJa5MLLSKEpeZJBRk-cFFTITPEMmKiHLbEyu1n2Xq7LByuAwTK2WnWt096m8dupvpXWvauE_lCiEZDSPDc43DTr_vsLQq8aFQU0U6VdBMQp8wuPHA_RsDV3oGpVrrR-ED3A1FVyCkJzJiLr4BxV3hY0zvkXr4vsfAqwJpvMhdGh_pweqBmPV2lgVjVWDsYpHzum27F_Gj5PZF9q_nVQ</recordid><startdate>20180315</startdate><enddate>20180315</enddate><creator>Perrin, Jackie</creator><creator>Bary, Aurélie</creator><creator>Vernay, Alexandre</creator><creator>Cosson, Pierre</creator><general>BioMed Central Ltd</general><general>BioMed Central</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><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1519-1244</orcidid></search><sort><creationdate>20180315</creationdate><title>Role of the HIV-1 envelope transmembrane domain in intracellular sorting</title><author>Perrin, Jackie ; Bary, Aurélie ; Vernay, Alexandre ; Cosson, Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-b92ff8b6f9fa0265444fcd40eec72fb75c6dae5b483130c7780563543e25d56b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - metabolism</topic><topic>Arginine</topic><topic>Causes of</topic><topic>Cell Membrane</topic><topic>Cellular proteins</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>env Gene Products, Human Immunodeficiency Virus - chemistry</topic><topic>env Gene Products, Human Immunodeficiency Virus - metabolism</topic><topic>HeLa Cells</topic><topic>HIV (Viruses)</topic><topic>HIV-1 - metabolism</topic><topic>Humans</topic><topic>Intracellular Space - metabolism</topic><topic>Lentivirus</topic><topic>Lentivirus - metabolism</topic><topic>Membrane proteins</topic><topic>Physiological aspects</topic><topic>Protein Domains</topic><topic>Protein Transport</topic><topic>Structure-Activity Relationship</topic><toplevel>online_resources</toplevel><creatorcontrib>Perrin, Jackie</creatorcontrib><creatorcontrib>Bary, Aurélie</creatorcontrib><creatorcontrib>Vernay, Alexandre</creatorcontrib><creatorcontrib>Cosson, Pierre</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>BMC cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perrin, Jackie</au><au>Bary, Aurélie</au><au>Vernay, Alexandre</au><au>Cosson, Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of the HIV-1 envelope transmembrane domain in intracellular sorting</atitle><jtitle>BMC cell biology</jtitle><addtitle>BMC Cell Biol</addtitle><date>2018-03-15</date><risdate>2018</risdate><volume>19</volume><issue>1</issue><spage>3</spage><epage>3</epage><pages>3-3</pages><artnum>3</artnum><issn>1471-2121</issn><eissn>1471-2121</eissn><abstract>The envelope protein of lentiviruses are type I transmembrane proteins, and their transmembrane domain contains conserved potentially charged residues. This highly unusual feature would be expected to cause endoplasmic reticulum (ER) localization. The aim of this study was to determine by which means the HIV-1 Env protein is transported to the cell surface although its transmembrane domain contains a conserved arginine residue.
We expressed various chimeric proteins and analyzed the influence of their transmembrane domain on their intracellular localization. The transmembrane domain of the HIV-1 Env protein does not cause ER retention. This is not due to the presence of conserved glycine residues, or to the position of the arginine residue, but to the length of the transmembrane domain. A shortened version of the Env transmembrane domain causes arginine-dependent ER targeting. Remarkably, the transmembrane domain of the HIV-1 Env protein, although it does not confer ER retention, interacts efficiently with negatively charged residues in the membrane.
These results suggest that the intrinsic properties of the HIV-1 Env transmembrane domain allow the protein to escape ER-retention mechanisms, while maintaining its ability to interact with cellular proteins and to influence cellular physiology.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>29544440</pmid><doi>10.1186/s12860-018-0153-4</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-1519-1244</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acids - metabolism Arginine Causes of Cell Membrane Cellular proteins Endoplasmic Reticulum - metabolism env Gene Products, Human Immunodeficiency Virus - chemistry env Gene Products, Human Immunodeficiency Virus - metabolism HeLa Cells HIV (Viruses) HIV-1 - metabolism Humans Intracellular Space - metabolism Lentivirus Lentivirus - metabolism Membrane proteins Physiological aspects Protein Domains Protein Transport Structure-Activity Relationship |
| title | Role of the HIV-1 envelope transmembrane domain in intracellular sorting |
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