Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium
Intracellular neutral lipid storage droplets are essential organelles of eukaryotic cells, yet little is known about the proteins at their surfaces or about the amino acid sequences that target proteins to these storage droplets. The mammalian proteins Perilipin, ADRP, and TIP47 share extensive amin...
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| Veröffentlicht in: | The Journal of biological chemistry 2002-08, Vol.277 (35), p.32253-32257 |
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| container_title | The Journal of biological chemistry |
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| creator | Miura, Shinji Gan, Jai-Wei Brzostowski, Joseph Parisi, Michael J Schultz, Charles J Londos, Constantine Oliver, Brian Kimmel, Alan R |
| description | Intracellular neutral lipid storage droplets are essential organelles of eukaryotic cells, yet little is known about the proteins
at their surfaces or about the amino acid sequences that target proteins to these storage droplets. The mammalian proteins
Perilipin, ADRP, and TIP47 share extensive amino acid sequence similarity, suggesting a common function. However, while Perilipin
and ADRP localize exclusively to neutral lipid storage droplets, an association of TIP47 with intracellular lipid droplets
has been controversial. We now show that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets. We have
also detected a close juxtaposition of TIP47 with the surfaces of lipid storage droplets using antibodies that specifically
recognize TIP47, further indicating that TIP47 associates with intracellular lipid storage droplets. Finally, we show that
related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophila lipid droplet surfaces in vivo . Thus, sequence and/or structural elements within this evolutionarily ancient protein family are necessary and sufficient
to direct association to heterologous intracellular lipid droplet surfaces, strongly indicating that they have a common function
for lipid deposition and/or mobilization. |
| doi_str_mv | 10.1074/jbc.M204410200 |
| format | Article |
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at their surfaces or about the amino acid sequences that target proteins to these storage droplets. The mammalian proteins
Perilipin, ADRP, and TIP47 share extensive amino acid sequence similarity, suggesting a common function. However, while Perilipin
and ADRP localize exclusively to neutral lipid storage droplets, an association of TIP47 with intracellular lipid droplets
has been controversial. We now show that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets. We have
also detected a close juxtaposition of TIP47 with the surfaces of lipid storage droplets using antibodies that specifically
recognize TIP47, further indicating that TIP47 associates with intracellular lipid storage droplets. Finally, we show that
related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophila lipid droplet surfaces in vivo . Thus, sequence and/or structural elements within this evolutionarily ancient protein family are necessary and sufficient
to direct association to heterologous intracellular lipid droplet surfaces, strongly indicating that they have a common function
for lipid deposition and/or mobilization.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M204410200</identifier><identifier>PMID: 12077142</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adipose Tissue - metabolism ; Animals ; Carrier Proteins ; CHO Cells ; Cricetinae ; Dictyostelium ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Drosophila ; Green Fluorescent Proteins ; Humans ; Intracellular Signaling Peptides and Proteins ; Luminescent Proteins - genetics ; Luminescent Proteins - metabolism ; Mammals ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Perilipin-1 ; Perilipin-2 ; Perilipin-3 ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Phylogeny ; Pregnancy Proteins ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; Species Specificity ; Vesicular Transport Proteins</subject><ispartof>The Journal of biological chemistry, 2002-08, Vol.277 (35), p.32253-32257</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-c1ae2aff6df0616b2fd8a8fb6d1d828e2b543d5931480747be36e7c68d3f41543</citedby><cites>FETCH-LOGICAL-c457t-c1ae2aff6df0616b2fd8a8fb6d1d828e2b543d5931480747be36e7c68d3f41543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12077142$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miura, Shinji</creatorcontrib><creatorcontrib>Gan, Jai-Wei</creatorcontrib><creatorcontrib>Brzostowski, Joseph</creatorcontrib><creatorcontrib>Parisi, Michael J</creatorcontrib><creatorcontrib>Schultz, Charles J</creatorcontrib><creatorcontrib>Londos, Constantine</creatorcontrib><creatorcontrib>Oliver, Brian</creatorcontrib><creatorcontrib>Kimmel, Alan R</creatorcontrib><title>Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Intracellular neutral lipid storage droplets are essential organelles of eukaryotic cells, yet little is known about the proteins
at their surfaces or about the amino acid sequences that target proteins to these storage droplets. The mammalian proteins
Perilipin, ADRP, and TIP47 share extensive amino acid sequence similarity, suggesting a common function. However, while Perilipin
and ADRP localize exclusively to neutral lipid storage droplets, an association of TIP47 with intracellular lipid droplets
has been controversial. We now show that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets. We have
also detected a close juxtaposition of TIP47 with the surfaces of lipid storage droplets using antibodies that specifically
recognize TIP47, further indicating that TIP47 associates with intracellular lipid storage droplets. Finally, we show that
related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophila lipid droplet surfaces in vivo . Thus, sequence and/or structural elements within this evolutionarily ancient protein family are necessary and sufficient
to direct association to heterologous intracellular lipid droplet surfaces, strongly indicating that they have a common function
for lipid deposition and/or mobilization.</description><subject>Adipose Tissue - metabolism</subject><subject>Animals</subject><subject>Carrier Proteins</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Dictyostelium</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila</subject><subject>Green Fluorescent Proteins</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Luminescent Proteins - genetics</subject><subject>Luminescent Proteins - metabolism</subject><subject>Mammals</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Perilipin-1</subject><subject>Perilipin-2</subject><subject>Perilipin-3</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Phylogeny</subject><subject>Pregnancy Proteins</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>Vesicular Transport Proteins</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U-L1DAYBvAgiju7evUoOYgoTMf8a9M5DjOuLsxi0RG8hTR5O5OlbWrSuuyX8bOapQN7NJcQ8nsfSB6E3lCyokSKT3e1Wd0yIgQljJBnaEFJyTOe01_P0YIQRrM1y8sLdBnjHUlLrOlLdEEZkZIKtkB_r6fejM73usVb30cIf_TjETc-4L0bnMU_Rh_0EfAu-KGFEW9i9MbNSne-P-IKgmuT7Zd4s_teLbHuLT7cVELiD9Xm8DEL0OoRLK6CH8H1Ebse3-qu021cptjoh5Nr9Ty3c2Z88HGE1k3dK_SiSQhen_cr9PP682H7Ndt_-3Kz3ewzI3I5ZoZqYLppCtuQghY1a2ypy6YuLLUlK4HVueA2X3MqyvRrsgZegDRFaXkjaLq7Qu_n3CH43xPEUXUuGmhb3YOfopKM8LzkxX8hLcVa5EwmuJqhSe-LARo1BNfp8KAoUY_VqVSdeqouDbw9J091B_aJn7tK4N0MTu54uncBVO28OUGnmJSK54ozlnP-D2ESoTw</recordid><startdate>20020830</startdate><enddate>20020830</enddate><creator>Miura, Shinji</creator><creator>Gan, Jai-Wei</creator><creator>Brzostowski, Joseph</creator><creator>Parisi, Michael J</creator><creator>Schultz, Charles J</creator><creator>Londos, Constantine</creator><creator>Oliver, Brian</creator><creator>Kimmel, Alan R</creator><general>American Society for Biochemistry and Molecular Biology</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>7SS</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20020830</creationdate><title>Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium</title><author>Miura, Shinji ; Gan, Jai-Wei ; Brzostowski, Joseph ; Parisi, Michael J ; Schultz, Charles J ; Londos, Constantine ; Oliver, Brian ; Kimmel, Alan R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-c1ae2aff6df0616b2fd8a8fb6d1d828e2b543d5931480747be36e7c68d3f41543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adipose Tissue - metabolism</topic><topic>Animals</topic><topic>Carrier Proteins</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Dictyostelium</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila</topic><topic>Green Fluorescent Proteins</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Luminescent Proteins - genetics</topic><topic>Luminescent Proteins - metabolism</topic><topic>Mammals</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Perilipin-1</topic><topic>Perilipin-2</topic><topic>Perilipin-3</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Phylogeny</topic><topic>Pregnancy Proteins</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miura, Shinji</creatorcontrib><creatorcontrib>Gan, Jai-Wei</creatorcontrib><creatorcontrib>Brzostowski, Joseph</creatorcontrib><creatorcontrib>Parisi, Michael J</creatorcontrib><creatorcontrib>Schultz, Charles J</creatorcontrib><creatorcontrib>Londos, Constantine</creatorcontrib><creatorcontrib>Oliver, Brian</creatorcontrib><creatorcontrib>Kimmel, Alan R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miura, Shinji</au><au>Gan, Jai-Wei</au><au>Brzostowski, Joseph</au><au>Parisi, Michael J</au><au>Schultz, Charles J</au><au>Londos, Constantine</au><au>Oliver, Brian</au><au>Kimmel, Alan R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-08-30</date><risdate>2002</risdate><volume>277</volume><issue>35</issue><spage>32253</spage><epage>32257</epage><pages>32253-32257</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Intracellular neutral lipid storage droplets are essential organelles of eukaryotic cells, yet little is known about the proteins
at their surfaces or about the amino acid sequences that target proteins to these storage droplets. The mammalian proteins
Perilipin, ADRP, and TIP47 share extensive amino acid sequence similarity, suggesting a common function. However, while Perilipin
and ADRP localize exclusively to neutral lipid storage droplets, an association of TIP47 with intracellular lipid droplets
has been controversial. We now show that GFP-tagged TIP47 co-localizes with isolated intracellular lipid droplets. We have
also detected a close juxtaposition of TIP47 with the surfaces of lipid storage droplets using antibodies that specifically
recognize TIP47, further indicating that TIP47 associates with intracellular lipid storage droplets. Finally, we show that
related proteins from species as diverse as Drosophila and Dictyostelium can also target mammalian or Drosophila lipid droplet surfaces in vivo . Thus, sequence and/or structural elements within this evolutionarily ancient protein family are necessary and sufficient
to direct association to heterologous intracellular lipid droplet surfaces, strongly indicating that they have a common function
for lipid deposition and/or mobilization.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>12077142</pmid><doi>10.1074/jbc.M204410200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2002-08, Vol.277 (35), p.32253-32257 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72035836 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adipose Tissue - metabolism Animals Carrier Proteins CHO Cells Cricetinae Dictyostelium DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Drosophila Green Fluorescent Proteins Humans Intracellular Signaling Peptides and Proteins Luminescent Proteins - genetics Luminescent Proteins - metabolism Mammals Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Perilipin-1 Perilipin-2 Perilipin-3 Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Phylogeny Pregnancy Proteins Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid Species Specificity Vesicular Transport Proteins |
| title | Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals,Drosophila, and Dictyostelium |
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