Cutinsomes and cuticle enzymes GPAT6 and DGAT2 seem to travel together from a lipotubuloid metabolon (LM) to extracellular matrix of O. umbellatum ovary epidermis
•Cutinsomes are nanoparticles participating in plant cuticle formation.•They are formed in cytoplasmic domain, lipotubuloid metabolon (LM), of O. umbellatum ovary epidermis and then translocated to aerial cell wall.•Cutinsomes may be platforms transporting cutin and wax synthesis enzymes, GPAT6 and...
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Veröffentlicht in: | Micron (Oxford, England : 1993) England : 1993), 2016-06, Vol.85, p.51-57 |
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creator | Stępiński, Dariusz Kwiatkowska, Maria Popłońska, Katarzyna Polit, Justyna T. Wojtczak, Agnieszka Domίnguez, Eva Heredia, Antonio |
description | •Cutinsomes are nanoparticles participating in plant cuticle formation.•They are formed in cytoplasmic domain, lipotubuloid metabolon (LM), of O. umbellatum ovary epidermis and then translocated to aerial cell wall.•Cutinsomes may be platforms transporting cutin and wax synthesis enzymes, GPAT6 and WS/DGAT2 respectively, from LM to cell wall.
In the ovary epidermis of O. umbellatum there are lipotubuloid metabolons (LMs), in which synthesis of lipids takes place. This process partly provides nourishment, and partly cuticle building blocks, transformed, among others, with the participation of cutinsomes. The cutinsomes are cutin-building structures, 40–200nm in size, which are formed as a result of self-assembly and self-esterification of hydroxy fatty acids. The cutinsomes, by binding to the cuticle, introduce into it nonlinear, amorphous and cross-linked polymers. Double-immunogold EM observations revealed that enzymes producing elements of cutin (GPAT6) and waxes (WS/DGAT) were found not only as free cytoplasmic molecules but also in many cases they were bound to carboxylate-carboxylic shell of cuntinsomes. Hence, we suppose that these enzymes can move alone or together with the cutinsomes through cytoplasm (pH 6.8–7.0), plasmalemma and the polysaccharide layer of a cell wall to the site of their functioning i.e. to the cuticle (pH 5.0). |
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In the ovary epidermis of O. umbellatum there are lipotubuloid metabolons (LMs), in which synthesis of lipids takes place. This process partly provides nourishment, and partly cuticle building blocks, transformed, among others, with the participation of cutinsomes. The cutinsomes are cutin-building structures, 40–200nm in size, which are formed as a result of self-assembly and self-esterification of hydroxy fatty acids. The cutinsomes, by binding to the cuticle, introduce into it nonlinear, amorphous and cross-linked polymers. Double-immunogold EM observations revealed that enzymes producing elements of cutin (GPAT6) and waxes (WS/DGAT) were found not only as free cytoplasmic molecules but also in many cases they were bound to carboxylate-carboxylic shell of cuntinsomes. Hence, we suppose that these enzymes can move alone or together with the cutinsomes through cytoplasm (pH 6.8–7.0), plasmalemma and the polysaccharide layer of a cell wall to the site of their functioning i.e. to the cuticle (pH 5.0).</description><identifier>ISSN: 0968-4328</identifier><identifier>EISSN: 1878-4291</identifier><identifier>DOI: 10.1016/j.micron.2016.04.002</identifier><identifier>PMID: 27088229</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Arabidopsis - enzymology ; Arabidopsis - physiology ; Cell Membrane - chemistry ; Cell Membrane - enzymology ; Cell Membrane - physiology ; Cell Wall - chemistry ; Cell Wall - enzymology ; Cell Wall - physiology ; Cuticle ; Cutinsomes ; Diacylglycerol O-Acyltransferase - metabolism ; Double-immunogold electron microscopy ; Enzymes ; Epidermis ; Extracellular Matrix - metabolism ; Fatty acids ; Flowers - metabolism ; Glycerol-3-Phosphate O-Acyltransferase - metabolism ; GPAT6 ; Liliaceae - enzymology ; Liliaceae - metabolism ; Lipid Metabolism ; Lipotubuloid metabolon ; Membrane Lipids - chemistry ; Nanoparticles - chemistry ; Ovaries ; Plant Epidermis - metabolism ; Plant Proteins - metabolism ; Self assembly ; Walls ; Wax ; WS/DGAT</subject><ispartof>Micron (Oxford, England : 1993), 2016-06, Vol.85, p.51-57</ispartof><rights>2016 Elsevier Ltd</rights><rights>Copyright © 2016 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c395t-c786a13b2ba616429df9de7f7923443bee5667e3f60a3f5f0e72e350a23d158b3</citedby><cites>FETCH-LOGICAL-c395t-c786a13b2ba616429df9de7f7923443bee5667e3f60a3f5f0e72e350a23d158b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0968432816300464$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27088229$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stępiński, Dariusz</creatorcontrib><creatorcontrib>Kwiatkowska, Maria</creatorcontrib><creatorcontrib>Popłońska, Katarzyna</creatorcontrib><creatorcontrib>Polit, Justyna T.</creatorcontrib><creatorcontrib>Wojtczak, Agnieszka</creatorcontrib><creatorcontrib>Domίnguez, Eva</creatorcontrib><creatorcontrib>Heredia, Antonio</creatorcontrib><title>Cutinsomes and cuticle enzymes GPAT6 and DGAT2 seem to travel together from a lipotubuloid metabolon (LM) to extracellular matrix of O. umbellatum ovary epidermis</title><title>Micron (Oxford, England : 1993)</title><addtitle>Micron</addtitle><description>•Cutinsomes are nanoparticles participating in plant cuticle formation.•They are formed in cytoplasmic domain, lipotubuloid metabolon (LM), of O. umbellatum ovary epidermis and then translocated to aerial cell wall.•Cutinsomes may be platforms transporting cutin and wax synthesis enzymes, GPAT6 and WS/DGAT2 respectively, from LM to cell wall.
In the ovary epidermis of O. umbellatum there are lipotubuloid metabolons (LMs), in which synthesis of lipids takes place. This process partly provides nourishment, and partly cuticle building blocks, transformed, among others, with the participation of cutinsomes. The cutinsomes are cutin-building structures, 40–200nm in size, which are formed as a result of self-assembly and self-esterification of hydroxy fatty acids. The cutinsomes, by binding to the cuticle, introduce into it nonlinear, amorphous and cross-linked polymers. Double-immunogold EM observations revealed that enzymes producing elements of cutin (GPAT6) and waxes (WS/DGAT) were found not only as free cytoplasmic molecules but also in many cases they were bound to carboxylate-carboxylic shell of cuntinsomes. Hence, we suppose that these enzymes can move alone or together with the cutinsomes through cytoplasm (pH 6.8–7.0), plasmalemma and the polysaccharide layer of a cell wall to the site of their functioning i.e. to the cuticle (pH 5.0).</description><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - physiology</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - enzymology</subject><subject>Cell Membrane - physiology</subject><subject>Cell Wall - chemistry</subject><subject>Cell Wall - enzymology</subject><subject>Cell Wall - physiology</subject><subject>Cuticle</subject><subject>Cutinsomes</subject><subject>Diacylglycerol O-Acyltransferase - metabolism</subject><subject>Double-immunogold electron microscopy</subject><subject>Enzymes</subject><subject>Epidermis</subject><subject>Extracellular Matrix - metabolism</subject><subject>Fatty acids</subject><subject>Flowers - metabolism</subject><subject>Glycerol-3-Phosphate O-Acyltransferase - metabolism</subject><subject>GPAT6</subject><subject>Liliaceae - enzymology</subject><subject>Liliaceae - metabolism</subject><subject>Lipid Metabolism</subject><subject>Lipotubuloid metabolon</subject><subject>Membrane Lipids - chemistry</subject><subject>Nanoparticles - chemistry</subject><subject>Ovaries</subject><subject>Plant Epidermis - metabolism</subject><subject>Plant Proteins - metabolism</subject><subject>Self assembly</subject><subject>Walls</subject><subject>Wax</subject><subject>WS/DGAT</subject><issn>0968-4328</issn><issn>1878-4291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQxi1ERbeFN0DIx3LY1P_iJBek1ZYuSIvKYTlbTjIBr-x4sZ1Vy-PwpHW6hSOcPDP-Ps94fgi9paSghMrrfeFMF_xYsJwVRBSEsBdoQeuqXgrW0JdoQRqZY87qc3QR454QQoUkr9A5q0hdM9Ys0O_1lMwYvYOI9djjLqedBQzjr4e5tvm62smnm5vNasdwBHA4eZyCPoLN0XdIPyDgIXiHNbbm4NPUTtabHjtIuvXWj_hq--X97IL77OvA2snqgJ1OwdxjP-C7Ak-uzXWdJof9UYcHDAfTQ3AmvkZng7YR3jyfl-jb7cfd-tNye7f5vF5tlx1vyrTsqlpqylvWakll3kA_ND1UQ9UwLgRvAUopK-CDJJoP5UCgYsBLohnvaVm3_BJdnd49BP9zgphUbj4Pq0fwU1S0ZqUQsqTi_9I8C2WykSxLxUmaWcUYYFCHYFz-oKJEzSDVXp1AqhmkIkJlkNn27rnD1Dro_5r-kMuCDycB5JUcDQQVOwNjB70J0CXVe_PvDo9ihrIi</recordid><startdate>201606</startdate><enddate>201606</enddate><creator>Stępiński, Dariusz</creator><creator>Kwiatkowska, Maria</creator><creator>Popłońska, Katarzyna</creator><creator>Polit, Justyna T.</creator><creator>Wojtczak, Agnieszka</creator><creator>Domίnguez, Eva</creator><creator>Heredia, Antonio</creator><general>Elsevier 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><scope>7SR</scope><scope>7U5</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>201606</creationdate><title>Cutinsomes and cuticle enzymes GPAT6 and DGAT2 seem to travel together from a lipotubuloid metabolon (LM) to extracellular matrix of O. umbellatum ovary epidermis</title><author>Stępiński, Dariusz ; Kwiatkowska, Maria ; Popłońska, Katarzyna ; Polit, Justyna T. ; Wojtczak, Agnieszka ; Domίnguez, Eva ; Heredia, Antonio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c395t-c786a13b2ba616429df9de7f7923443bee5667e3f60a3f5f0e72e350a23d158b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - physiology</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - enzymology</topic><topic>Cell Membrane - physiology</topic><topic>Cell Wall - chemistry</topic><topic>Cell Wall - enzymology</topic><topic>Cell Wall - physiology</topic><topic>Cuticle</topic><topic>Cutinsomes</topic><topic>Diacylglycerol O-Acyltransferase - metabolism</topic><topic>Double-immunogold electron microscopy</topic><topic>Enzymes</topic><topic>Epidermis</topic><topic>Extracellular Matrix - metabolism</topic><topic>Fatty acids</topic><topic>Flowers - metabolism</topic><topic>Glycerol-3-Phosphate O-Acyltransferase - metabolism</topic><topic>GPAT6</topic><topic>Liliaceae - enzymology</topic><topic>Liliaceae - metabolism</topic><topic>Lipid Metabolism</topic><topic>Lipotubuloid metabolon</topic><topic>Membrane Lipids - chemistry</topic><topic>Nanoparticles - chemistry</topic><topic>Ovaries</topic><topic>Plant Epidermis - metabolism</topic><topic>Plant Proteins - metabolism</topic><topic>Self assembly</topic><topic>Walls</topic><topic>Wax</topic><topic>WS/DGAT</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stępiński, Dariusz</creatorcontrib><creatorcontrib>Kwiatkowska, Maria</creatorcontrib><creatorcontrib>Popłońska, Katarzyna</creatorcontrib><creatorcontrib>Polit, Justyna T.</creatorcontrib><creatorcontrib>Wojtczak, Agnieszka</creatorcontrib><creatorcontrib>Domίnguez, Eva</creatorcontrib><creatorcontrib>Heredia, Antonio</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>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Micron (Oxford, England : 1993)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stępiński, Dariusz</au><au>Kwiatkowska, Maria</au><au>Popłońska, Katarzyna</au><au>Polit, Justyna T.</au><au>Wojtczak, Agnieszka</au><au>Domίnguez, Eva</au><au>Heredia, Antonio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cutinsomes and cuticle enzymes GPAT6 and DGAT2 seem to travel together from a lipotubuloid metabolon (LM) to extracellular matrix of O. umbellatum ovary epidermis</atitle><jtitle>Micron (Oxford, England : 1993)</jtitle><addtitle>Micron</addtitle><date>2016-06</date><risdate>2016</risdate><volume>85</volume><spage>51</spage><epage>57</epage><pages>51-57</pages><issn>0968-4328</issn><eissn>1878-4291</eissn><abstract>•Cutinsomes are nanoparticles participating in plant cuticle formation.•They are formed in cytoplasmic domain, lipotubuloid metabolon (LM), of O. umbellatum ovary epidermis and then translocated to aerial cell wall.•Cutinsomes may be platforms transporting cutin and wax synthesis enzymes, GPAT6 and WS/DGAT2 respectively, from LM to cell wall.
In the ovary epidermis of O. umbellatum there are lipotubuloid metabolons (LMs), in which synthesis of lipids takes place. This process partly provides nourishment, and partly cuticle building blocks, transformed, among others, with the participation of cutinsomes. The cutinsomes are cutin-building structures, 40–200nm in size, which are formed as a result of self-assembly and self-esterification of hydroxy fatty acids. The cutinsomes, by binding to the cuticle, introduce into it nonlinear, amorphous and cross-linked polymers. Double-immunogold EM observations revealed that enzymes producing elements of cutin (GPAT6) and waxes (WS/DGAT) were found not only as free cytoplasmic molecules but also in many cases they were bound to carboxylate-carboxylic shell of cuntinsomes. Hence, we suppose that these enzymes can move alone or together with the cutinsomes through cytoplasm (pH 6.8–7.0), plasmalemma and the polysaccharide layer of a cell wall to the site of their functioning i.e. to the cuticle (pH 5.0).</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>27088229</pmid><doi>10.1016/j.micron.2016.04.002</doi><tpages>7</tpages></addata></record> |
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subjects | Arabidopsis - enzymology Arabidopsis - physiology Cell Membrane - chemistry Cell Membrane - enzymology Cell Membrane - physiology Cell Wall - chemistry Cell Wall - enzymology Cell Wall - physiology Cuticle Cutinsomes Diacylglycerol O-Acyltransferase - metabolism Double-immunogold electron microscopy Enzymes Epidermis Extracellular Matrix - metabolism Fatty acids Flowers - metabolism Glycerol-3-Phosphate O-Acyltransferase - metabolism GPAT6 Liliaceae - enzymology Liliaceae - metabolism Lipid Metabolism Lipotubuloid metabolon Membrane Lipids - chemistry Nanoparticles - chemistry Ovaries Plant Epidermis - metabolism Plant Proteins - metabolism Self assembly Walls Wax WS/DGAT |
title | Cutinsomes and cuticle enzymes GPAT6 and DGAT2 seem to travel together from a lipotubuloid metabolon (LM) to extracellular matrix of O. umbellatum ovary epidermis |
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