Conserved N- and C-terminal motifs of PAD-1 are required to inhibit extracellular vesicle release
The Dopey family protein PAD-1 is a key regulator of extracellular vesicle (EV) release in Caenorhabditis elegans (Beer et al., 2018; Fazeli et al., 2020). PAD-1 is thought to inhibit EV release by activating the phospholipid flippase TAT-5 to maintain phosphatidylethanolamine (PE) asymmetry in the...
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description | The Dopey family protein PAD-1 is a key regulator of extracellular vesicle (EV) release in Caenorhabditis elegans (Beer et al., 2018; Fazeli et al., 2020). PAD-1 is thought to inhibit EV release by activating the phospholipid flippase TAT-5 to maintain phosphatidylethanolamine (PE) asymmetry in the plasma membrane. When PAD-1 is disrupted, cytofacial PE is externalized, membrane-sculpting ESCRT complexes are recruited to the plasma membrane, and EVs bud from the plasma membrane by ectocytosis (Beer et al., 2018; Beer, 2021). However, which domains of PAD-1 are important to regulate EV release was unknown. |
doi_str_mv | 10.17912/micropub.biology.000625 |
format | Article |
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PAD-1 is thought to inhibit EV release by activating the phospholipid flippase TAT-5 to maintain phosphatidylethanolamine (PE) asymmetry in the plasma membrane. When PAD-1 is disrupted, cytofacial PE is externalized, membrane-sculpting ESCRT complexes are recruited to the plasma membrane, and EVs bud from the plasma membrane by ectocytosis (Beer et al., 2018; Beer, 2021). However, which domains of PAD-1 are important to regulate EV release was unknown.</description><identifier>EISSN: 2578-9430</identifier><identifier>DOI: 10.17912/micropub.biology.000625</identifier><language>eng</language><publisher>microPublication Biology</publisher><subject>C. 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PAD-1 is thought to inhibit EV release by activating the phospholipid flippase TAT-5 to maintain phosphatidylethanolamine (PE) asymmetry in the plasma membrane. When PAD-1 is disrupted, cytofacial PE is externalized, membrane-sculpting ESCRT complexes are recruited to the plasma membrane, and EVs bud from the plasma membrane by ectocytosis (Beer et al., 2018; Beer, 2021). However, which domains of PAD-1 are important to regulate EV release was unknown.</description><subject>C. 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Elegans</topic><topic>Genotype Data</topic><topic>New Finding</topic><topic>Phenotype Data</topic><toplevel>peer_reviewed</toplevel><creatorcontrib>Pitts, Lauren R</creatorcontrib><creatorcontrib>Nguyen, Alexander T</creatorcontrib><creatorcontrib>Wehman, Ann M</creatorcontrib><collection>DataCite</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>microPublication biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>no_fulltext_linktorsrc</fulltext></delivery><addata><au>Pitts, Lauren R</au><au>Nguyen, Alexander T</au><au>Wehman, Ann M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conserved N- and C-terminal motifs of PAD-1 are required to inhibit extracellular vesicle release</atitle><jtitle>microPublication biology</jtitle><date>2022-01-01</date><risdate>2022</risdate><volume>2022</volume><eissn>2578-9430</eissn><abstract>The Dopey family protein PAD-1 is a key regulator of extracellular vesicle (EV) release in Caenorhabditis elegans (Beer et al., 2018; Fazeli et al., 2020). PAD-1 is thought to inhibit EV release by activating the phospholipid flippase TAT-5 to maintain phosphatidylethanolamine (PE) asymmetry in the plasma membrane. When PAD-1 is disrupted, cytofacial PE is externalized, membrane-sculpting ESCRT complexes are recruited to the plasma membrane, and EVs bud from the plasma membrane by ectocytosis (Beer et al., 2018; Beer, 2021). However, which domains of PAD-1 are important to regulate EV release was unknown.</abstract><pub>microPublication Biology</pub><doi>10.17912/micropub.biology.000625</doi><oa>free_for_read</oa></addata></record> |
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subjects | C. Elegans Genotype Data New Finding Phenotype Data |
title | Conserved N- and C-terminal motifs of PAD-1 are required to inhibit extracellular vesicle release |
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