Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm of mouse embryos
The small GTPase Arl8b localizes primarily to lysosomes and is involved in lysosomal motility and fusion. Here, we show that Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm (VYSE), an apical cell layer of the visceral yolk sac, of mouse embryos. The...
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| Veröffentlicht in: | Journal of cell science 2017-10, Vol.130 (20), p.3568-3577 |
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| creator | Oka, Miho Hashimoto, Keisuke Yamaguchi, Yoshifumi Saitoh, Shin-Ichiro Sugiura, Yuki Motoi, Yuji Honda, Kurara Kikko, Yorifumi Ohata, Shinya Suematsu, Makoto Miura, Masayuki Miyake, Kensuke Katada, Toshiaki Kontani, Kenji |
| description | The small GTPase Arl8b localizes primarily to lysosomes and is involved in lysosomal motility and fusion. Here, we show that Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm (VYSE), an apical cell layer of the visceral yolk sac, of mouse embryos. The VYSE actively takes up maternal materials from uterine fluid and degrades them in lysosomes to provide breakdown products to the embryo. Arl8b gene-trap mice (
) displayed decreased early embryo body size. The
VYSE exhibited defective endocytic trafficking to the lysosome and accumulation of maternal proteins such as albumin and immunoglobulin G in late endocytic organelles. Furthermore,
mice in which Arl8b was ablated specifically in the VYSE also showed decreased embryo body size, defects in trafficking to the lysosome and reduction of the free amino acid level in the embryos. Taken together, these results suggest that Arl8b mediates lysosomal degradation of maternal proteins in the VYSE, thereby contributing to mouse embryonic development. |
| doi_str_mv | 10.1242/jcs.200519 |
| format | Article |
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) displayed decreased early embryo body size. The
VYSE exhibited defective endocytic trafficking to the lysosome and accumulation of maternal proteins such as albumin and immunoglobulin G in late endocytic organelles. Furthermore,
mice in which Arl8b was ablated specifically in the VYSE also showed decreased embryo body size, defects in trafficking to the lysosome and reduction of the free amino acid level in the embryos. Taken together, these results suggest that Arl8b mediates lysosomal degradation of maternal proteins in the VYSE, thereby contributing to mouse embryonic development.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.200519</identifier><identifier>PMID: 28827407</identifier><language>eng</language><publisher>England: The Company of Biologists Ltd</publisher><subject>ADP-Ribosylation Factors - physiology ; Amino acids ; Animals ; Auditory defects ; Body size ; Degradation ; Embryo, Mammalian - metabolism ; Embryogenesis ; Embryonic growth stage ; Embryos ; Endoderm ; Female ; Flox ; Guanosine triphosphatases ; Immunoglobulin G ; Lysosomes ; Lysosomes - metabolism ; Mice ; Mice, Inbred C57BL ; Organelles ; Protein transport ; Proteins ; Proteolysis ; Transthyretin ; Uterus ; Yolk ; Yolk sac ; Yolk Sac - metabolism</subject><ispartof>Journal of cell science, 2017-10, Vol.130 (20), p.3568-3577</ispartof><rights>2017. Published by The Company of Biologists Ltd.</rights><rights>Copyright The Company of Biologists Ltd Oct 15, 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-547328022420424e758e4c74674614f4e02dd230b5d0d1f968e47427e489a8683</citedby><cites>FETCH-LOGICAL-c417t-547328022420424e758e4c74674614f4e02dd230b5d0d1f968e47427e489a8683</cites><orcidid>0000-0001-7122-0877</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28827407$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oka, Miho</creatorcontrib><creatorcontrib>Hashimoto, Keisuke</creatorcontrib><creatorcontrib>Yamaguchi, Yoshifumi</creatorcontrib><creatorcontrib>Saitoh, Shin-Ichiro</creatorcontrib><creatorcontrib>Sugiura, Yuki</creatorcontrib><creatorcontrib>Motoi, Yuji</creatorcontrib><creatorcontrib>Honda, Kurara</creatorcontrib><creatorcontrib>Kikko, Yorifumi</creatorcontrib><creatorcontrib>Ohata, Shinya</creatorcontrib><creatorcontrib>Suematsu, Makoto</creatorcontrib><creatorcontrib>Miura, Masayuki</creatorcontrib><creatorcontrib>Miyake, Kensuke</creatorcontrib><creatorcontrib>Katada, Toshiaki</creatorcontrib><creatorcontrib>Kontani, Kenji</creatorcontrib><title>Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm of mouse embryos</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>The small GTPase Arl8b localizes primarily to lysosomes and is involved in lysosomal motility and fusion. Here, we show that Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm (VYSE), an apical cell layer of the visceral yolk sac, of mouse embryos. The VYSE actively takes up maternal materials from uterine fluid and degrades them in lysosomes to provide breakdown products to the embryo. Arl8b gene-trap mice (
) displayed decreased early embryo body size. The
VYSE exhibited defective endocytic trafficking to the lysosome and accumulation of maternal proteins such as albumin and immunoglobulin G in late endocytic organelles. Furthermore,
mice in which Arl8b was ablated specifically in the VYSE also showed decreased embryo body size, defects in trafficking to the lysosome and reduction of the free amino acid level in the embryos. Taken together, these results suggest that Arl8b mediates lysosomal degradation of maternal proteins in the VYSE, thereby contributing to mouse embryonic development.</description><subject>ADP-Ribosylation Factors - physiology</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Auditory defects</subject><subject>Body size</subject><subject>Degradation</subject><subject>Embryo, Mammalian - metabolism</subject><subject>Embryogenesis</subject><subject>Embryonic growth stage</subject><subject>Embryos</subject><subject>Endoderm</subject><subject>Female</subject><subject>Flox</subject><subject>Guanosine triphosphatases</subject><subject>Immunoglobulin G</subject><subject>Lysosomes</subject><subject>Lysosomes - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Organelles</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Transthyretin</subject><subject>Uterus</subject><subject>Yolk</subject><subject>Yolk sac</subject><subject>Yolk Sac - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1Lw0AQhhdRbK1e_AGy4EWE1P1KdnMsxS8oeNFz2GYnmppk251E6L93a6sHYWBg5pnhnXkJueRsyoUSd6sSp4KxlOdHZMyV1knOpT4mY8YET_JUyhE5Q1wxxrTI9SkZCWOEVkyPCc5CY5a0RhpgM9QBHK18oM0WPfrWNtTBe7DO9rXvqK9oa3sIXayvg--h7pDWHe0_gH7VWEKIja1vPinakkLnvIPQ_oz5AYFCuwxbj-fkpLINwsUhT8jbw_3r_ClZvDw-z2eLpFRc90mqtBSGiXgiU0KBTg2oUqssBleVAiacE5ItU8ccr_IstrUSGpTJrcmMnJCb_d6odTMA9kW7E9k0toOop-C55EJmmdYRvf6Hrvywu3NHGalkVCQidbunyuARA1TFOtStDduCs2JnRRGtKPZWRPjqsHJYtuD-0N_fy2_BxYMB</recordid><startdate>20171015</startdate><enddate>20171015</enddate><creator>Oka, Miho</creator><creator>Hashimoto, Keisuke</creator><creator>Yamaguchi, Yoshifumi</creator><creator>Saitoh, Shin-Ichiro</creator><creator>Sugiura, Yuki</creator><creator>Motoi, Yuji</creator><creator>Honda, Kurara</creator><creator>Kikko, Yorifumi</creator><creator>Ohata, Shinya</creator><creator>Suematsu, Makoto</creator><creator>Miura, Masayuki</creator><creator>Miyake, Kensuke</creator><creator>Katada, Toshiaki</creator><creator>Kontani, Kenji</creator><general>The Company of Biologists 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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-7122-0877</orcidid></search><sort><creationdate>20171015</creationdate><title>Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm of mouse embryos</title><author>Oka, Miho ; 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Here, we show that Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm (VYSE), an apical cell layer of the visceral yolk sac, of mouse embryos. The VYSE actively takes up maternal materials from uterine fluid and degrades them in lysosomes to provide breakdown products to the embryo. Arl8b gene-trap mice (
) displayed decreased early embryo body size. The
VYSE exhibited defective endocytic trafficking to the lysosome and accumulation of maternal proteins such as albumin and immunoglobulin G in late endocytic organelles. Furthermore,
mice in which Arl8b was ablated specifically in the VYSE also showed decreased embryo body size, defects in trafficking to the lysosome and reduction of the free amino acid level in the embryos. Taken together, these results suggest that Arl8b mediates lysosomal degradation of maternal proteins in the VYSE, thereby contributing to mouse embryonic development.</abstract><cop>England</cop><pub>The Company of Biologists Ltd</pub><pmid>28827407</pmid><doi>10.1242/jcs.200519</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-7122-0877</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of cell science, 2017-10, Vol.130 (20), p.3568-3577 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; Company of Biologists |
| subjects | ADP-Ribosylation Factors - physiology Amino acids Animals Auditory defects Body size Degradation Embryo, Mammalian - metabolism Embryogenesis Embryonic growth stage Embryos Endoderm Female Flox Guanosine triphosphatases Immunoglobulin G Lysosomes Lysosomes - metabolism Mice Mice, Inbred C57BL Organelles Protein transport Proteins Proteolysis Transthyretin Uterus Yolk Yolk sac Yolk Sac - metabolism |
| title | Arl8b is required for lysosomal degradation of maternal proteins in the visceral yolk sac endoderm of mouse embryos |
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