SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation
SLC10A7, encoded by the so-called SLC10A7 gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is...
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| Veröffentlicht in: | Human genetics 2022-07, Vol.141 (7), p.1287-1298 |
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| creator | Durin, Zoé Dubail, Johanne Layotte, Aurore Legrand, Dominique Cormier-Daire, Valérie Foulquier, François |
| description | SLC10A7, encoded by the so-called
SLC10A7
gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is then considered yet as an orphan carrier. Recently,
SLC10A7
mutations have been identified as responsible for a new Congenital Disorder of Glycosylation (CDG). CDG are a family of rare and inherited metabolic disorders, where glycosylation abnormalities lead to multisystemic defects. SLC10A7-CDG patients presented skeletal dysplasia with multiple large joint dislocations, short stature and
amelogenesis imperfecta
likely mediated by glycosaminoglycan (GAG) defects
.
Although it has been demonstrated that the transporter and substrate specificities of SLC10A7, if any, differ from those of the main members of the protein family, SLC10A7 seems to play a role in Ca
2+
regulation and is involved in proper glycosaminoglycan biosynthesis, especially heparan-sulfate, and N-glycosylation. This paper will review our current knowledge on the known and predicted structural and functional properties of this fascinating protein, and its link with the glycosylation process. |
| doi_str_mv | 10.1007/s00439-021-02420-x |
| format | Article |
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SLC10A7
gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is then considered yet as an orphan carrier. Recently,
SLC10A7
mutations have been identified as responsible for a new Congenital Disorder of Glycosylation (CDG). CDG are a family of rare and inherited metabolic disorders, where glycosylation abnormalities lead to multisystemic defects. SLC10A7-CDG patients presented skeletal dysplasia with multiple large joint dislocations, short stature and
amelogenesis imperfecta
likely mediated by glycosaminoglycan (GAG) defects
.
Although it has been demonstrated that the transporter and substrate specificities of SLC10A7, if any, differ from those of the main members of the protein family, SLC10A7 seems to play a role in Ca
2+
regulation and is involved in proper glycosaminoglycan biosynthesis, especially heparan-sulfate, and N-glycosylation. This paper will review our current knowledge on the known and predicted structural and functional properties of this fascinating protein, and its link with the glycosylation process.</description><identifier>ISSN: 0340-6717</identifier><identifier>EISSN: 1432-1203</identifier><identifier>DOI: 10.1007/s00439-021-02420-x</identifier><identifier>PMID: 34999954</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amelogenesis imperfecta ; Biochemistry, Molecular Biology ; Biomedical and Life Sciences ; Biomedicine ; Bone dysplasia ; Congenital diseases ; Dysplasia ; Gene Function ; Genetic aspects ; Genetic disorders ; Genetics ; Glycosaminoglycans ; Glycosylation ; Human Genetics ; Inherited errors of metabolism ; Life Sciences ; Metabolic Diseases ; Metabolic disorders ; Molecular Medicine ; Original Article ; Physiological aspects ; Skeleton ; Structure-function relationships</subject><ispartof>Human genetics, 2022-07, Vol.141 (7), p.1287-1298</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2022</rights><rights>2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><rights>COPYRIGHT 2022 Springer</rights><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2022.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-46a029e51c46e6a31cd4b717fd5703bc1f3215ff6e34b3ff9ae0ae8a7aa812a23</citedby><cites>FETCH-LOGICAL-c554t-46a029e51c46e6a31cd4b717fd5703bc1f3215ff6e34b3ff9ae0ae8a7aa812a23</cites><orcidid>0000-0002-0814-221X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00439-021-02420-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00439-021-02420-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34999954$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.univ-lille.fr/hal-03538979$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Durin, Zoé</creatorcontrib><creatorcontrib>Dubail, Johanne</creatorcontrib><creatorcontrib>Layotte, Aurore</creatorcontrib><creatorcontrib>Legrand, Dominique</creatorcontrib><creatorcontrib>Cormier-Daire, Valérie</creatorcontrib><creatorcontrib>Foulquier, François</creatorcontrib><title>SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation</title><title>Human genetics</title><addtitle>Hum Genet</addtitle><addtitle>Hum Genet</addtitle><description>SLC10A7, encoded by the so-called
SLC10A7
gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is then considered yet as an orphan carrier. Recently,
SLC10A7
mutations have been identified as responsible for a new Congenital Disorder of Glycosylation (CDG). CDG are a family of rare and inherited metabolic disorders, where glycosylation abnormalities lead to multisystemic defects. SLC10A7-CDG patients presented skeletal dysplasia with multiple large joint dislocations, short stature and
amelogenesis imperfecta
likely mediated by glycosaminoglycan (GAG) defects
.
Although it has been demonstrated that the transporter and substrate specificities of SLC10A7, if any, differ from those of the main members of the protein family, SLC10A7 seems to play a role in Ca
2+
regulation and is involved in proper glycosaminoglycan biosynthesis, especially heparan-sulfate, and N-glycosylation. This paper will review our current knowledge on the known and predicted structural and functional properties of this fascinating protein, and its link with the glycosylation process.</description><subject>Amelogenesis imperfecta</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bone dysplasia</subject><subject>Congenital diseases</subject><subject>Dysplasia</subject><subject>Gene Function</subject><subject>Genetic aspects</subject><subject>Genetic disorders</subject><subject>Genetics</subject><subject>Glycosaminoglycans</subject><subject>Glycosylation</subject><subject>Human Genetics</subject><subject>Inherited errors of metabolism</subject><subject>Life Sciences</subject><subject>Metabolic Diseases</subject><subject>Metabolic disorders</subject><subject>Molecular Medicine</subject><subject>Original Article</subject><subject>Physiological aspects</subject><subject>Skeleton</subject><subject>Structure-function relationships</subject><issn>0340-6717</issn><issn>1432-1203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kl1rFDEUhoModlv9A17IgDcWnJrP-bhcFm0LC4LV65CdOdlNyUzWZGbZ_fee7dSWFTEhnJA87yHn5CXkHaNXjNLyc6JUijqnnOGSnOb7F2TGpOA541S8JDMqJM2LkpVn5Dyle0qZqrl6Tc6ErHEoOSP6brlgdF5-ykyfhbjdYOigW0HMgs2GDWQPQGZN5_whc_0u-B20uMma0K-hd4PxWetSiC3EdBSt_aEJ6eDN4EL_hryyxid4-xgvyM-vX34sbvLlt-vbxXyZN0rJIZeFobwGxRpZQGEEa1q5wofbVpVUrBpmBWfK2gKEXAlrawPUQGVKYyrGDRcX5HLKuzFeb6PrTDzoYJy-mS_18YwKJaq6rHcM2Y8Tu43h1whp0J1LDXhveghj0rxglWIVNgjRD3-h92GMPVaCVKUqJnnFnqm18aBdb8MQTXNMquclrVWhpCyQuvoHhbOFzmEzwTo8PxFcngiQGWA_rM2Ykr69-37K8oltYkgpgn1qAqP66BY9uUWjW_SDW_QeRe8fqxtXHbRPkj_2QEBMQMIr_O34XP5_0v4G89PF9g</recordid><startdate>20220701</startdate><enddate>20220701</enddate><creator>Durin, Zoé</creator><creator>Dubail, Johanne</creator><creator>Layotte, Aurore</creator><creator>Legrand, Dominique</creator><creator>Cormier-Daire, Valérie</creator><creator>Foulquier, François</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><general>Springer Verlag</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-0814-221X</orcidid></search><sort><creationdate>20220701</creationdate><title>SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation</title><author>Durin, Zoé ; 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SLC10A7
gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is then considered yet as an orphan carrier. Recently,
SLC10A7
mutations have been identified as responsible for a new Congenital Disorder of Glycosylation (CDG). CDG are a family of rare and inherited metabolic disorders, where glycosylation abnormalities lead to multisystemic defects. SLC10A7-CDG patients presented skeletal dysplasia with multiple large joint dislocations, short stature and
amelogenesis imperfecta
likely mediated by glycosaminoglycan (GAG) defects
.
Although it has been demonstrated that the transporter and substrate specificities of SLC10A7, if any, differ from those of the main members of the protein family, SLC10A7 seems to play a role in Ca
2+
regulation and is involved in proper glycosaminoglycan biosynthesis, especially heparan-sulfate, and N-glycosylation. This paper will review our current knowledge on the known and predicted structural and functional properties of this fascinating protein, and its link with the glycosylation process.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>34999954</pmid><doi>10.1007/s00439-021-02420-x</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-0814-221X</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Human genetics, 2022-07, Vol.141 (7), p.1287-1298 |
| issn | 0340-6717 1432-1203 |
| language | eng |
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| source | SpringerLink Journals |
| subjects | Amelogenesis imperfecta Biochemistry, Molecular Biology Biomedical and Life Sciences Biomedicine Bone dysplasia Congenital diseases Dysplasia Gene Function Genetic aspects Genetic disorders Genetics Glycosaminoglycans Glycosylation Human Genetics Inherited errors of metabolism Life Sciences Metabolic Diseases Metabolic disorders Molecular Medicine Original Article Physiological aspects Skeleton Structure-function relationships |
| title | SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation |
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