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Structure, function, and pathology of protein O-glucosyltransferases
Protein O -glucosylation is a crucial form of O -glycosylation, which involves glucose (Glc) addition to a serine residue within a consensus sequence of epidermal growth factor epidermal growth factor (EGF)-like repeats found in several proteins, including Notch. Glc provides stability to EGF-like r...
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Published in: | Cell death & disease 2021-01, Vol.12 (1), p.71-71, Article 71 |
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description | Protein
O
-glucosylation is a crucial form of
O
-glycosylation, which involves glucose (Glc) addition to a serine residue within a consensus sequence of epidermal growth factor epidermal growth factor (EGF)-like repeats found in several proteins, including Notch. Glc provides stability to EGF-like repeats, is required for S2 cleavage of Notch, and serves to regulate the trafficking of Notch, crumbs2, and Eyes shut proteins to the cell surface. Genetic and biochemical studies have shown a link between aberrant protein
O
-glucosylation and human diseases. The main players of protein
O-
glucosylation, protein
O
-glucosyltransferases (POGLUTs), use uridine diphosphate (UDP)-Glc as a substrate to modify EGF repeats and reside in the endoplasmic reticulum via C-terminal KDEL-like signals. In addition to
O
-glucosylation activity, POGLUTs can also perform protein
O
-xylosylation function, i.e., adding xylose (Xyl) from UDP-Xyl; however, both activities rely on residues of EGF repeats, active-site conformations of POGLUTs and sugar substrate concentrations in the ER. Impaired expression of POGLUTs has been associated with initiation and progression of human diseases such as limb-girdle muscular dystrophy, Dowling–Degos disease 4, acute myeloid leukemia, and hepatocytes and pancreatic dysfunction. POGLUTs have been found to alter the expression of cyclin-dependent kinase inhibitors (CDKIs), by affecting Notch or transforming growth factor-β1 signaling, and cause cell proliferation inhibition or induction depending on the particular cell types, which characterizes POGLUT’s cell-dependent dual role. Except for a few downstream elements, the precise mechanisms whereby aberrant protein
O
-glucosylation causes diseases are largely unknown, leaving behind many questions that need to be addressed. This systemic review comprehensively covers literature to understand the
O
-glucosyltransferases with a focus on POGLUT1 structure and function, and their role in health and diseases. Moreover, this study also raises unanswered issues for future research in cancer biology, cell communications, muscular diseases, etc. |
doi_str_mv | 10.1038/s41419-020-03314-y |
format | article |
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O
-glucosylation is a crucial form of
O
-glycosylation, which involves glucose (Glc) addition to a serine residue within a consensus sequence of epidermal growth factor epidermal growth factor (EGF)-like repeats found in several proteins, including Notch. Glc provides stability to EGF-like repeats, is required for S2 cleavage of Notch, and serves to regulate the trafficking of Notch, crumbs2, and Eyes shut proteins to the cell surface. Genetic and biochemical studies have shown a link between aberrant protein
O
-glucosylation and human diseases. The main players of protein
O-
glucosylation, protein
O
-glucosyltransferases (POGLUTs), use uridine diphosphate (UDP)-Glc as a substrate to modify EGF repeats and reside in the endoplasmic reticulum via C-terminal KDEL-like signals. In addition to
O
-glucosylation activity, POGLUTs can also perform protein
O
-xylosylation function, i.e., adding xylose (Xyl) from UDP-Xyl; however, both activities rely on residues of EGF repeats, active-site conformations of POGLUTs and sugar substrate concentrations in the ER. Impaired expression of POGLUTs has been associated with initiation and progression of human diseases such as limb-girdle muscular dystrophy, Dowling–Degos disease 4, acute myeloid leukemia, and hepatocytes and pancreatic dysfunction. POGLUTs have been found to alter the expression of cyclin-dependent kinase inhibitors (CDKIs), by affecting Notch or transforming growth factor-β1 signaling, and cause cell proliferation inhibition or induction depending on the particular cell types, which characterizes POGLUT’s cell-dependent dual role. Except for a few downstream elements, the precise mechanisms whereby aberrant protein
O
-glucosylation causes diseases are largely unknown, leaving behind many questions that need to be addressed. This systemic review comprehensively covers literature to understand the
O
-glucosyltransferases with a focus on POGLUT1 structure and function, and their role in health and diseases. Moreover, this study also raises unanswered issues for future research in cancer biology, cell communications, muscular diseases, etc.</description><identifier>ISSN: 2041-4889</identifier><identifier>EISSN: 2041-4889</identifier><identifier>DOI: 10.1038/s41419-020-03314-y</identifier><identifier>PMID: 33436558</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 13/1 ; 13/51 ; 13/89 ; 38 ; 38/35 ; 38/70 ; 631/80/458/1524 ; 64 ; 64/24 ; 64/60 ; 692/699/67/395 ; Acute myeloid leukemia ; Antibodies ; Biochemistry ; Biomedical and Life Sciences ; Cell Biology ; Cell Culture ; Cell proliferation ; Cell surface ; Conserved sequence ; Cyclin-dependent kinase ; Cyclin-dependent kinase inhibitors ; Cyclin-dependent kinases ; Endoplasmic reticulum ; Epidermal growth factor ; Glucosyltransferases - metabolism ; Glycosylation ; Hepatocytes ; Humans ; Immunology ; Kinases ; Life Sciences ; Muscular diseases ; Muscular dystrophy ; Myeloid leukemia ; Oncogenes - physiology ; Pancreas ; Proteins ; Review ; Review Article ; Serine ; Structure-function relationships ; Uridine</subject><ispartof>Cell death & disease, 2021-01, Vol.12 (1), p.71-71, Article 71</ispartof><rights>The Author(s) 2021</rights><rights>The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c540t-e5ae9bf67bb6bc8cffc6998911dff516d262466913eaf1c9afbcd9730363dcb53</citedby><cites>FETCH-LOGICAL-c540t-e5ae9bf67bb6bc8cffc6998911dff516d262466913eaf1c9afbcd9730363dcb53</cites><orcidid>0000-0003-3801-2675</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2477091715/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2477091715?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33436558$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mehboob, Muhammad Zubair</creatorcontrib><creatorcontrib>Lang, Minglin</creatorcontrib><title>Structure, function, and pathology of protein O-glucosyltransferases</title><title>Cell death & disease</title><addtitle>Cell Death Dis</addtitle><addtitle>Cell Death Dis</addtitle><description>Protein
O
-glucosylation is a crucial form of
O
-glycosylation, which involves glucose (Glc) addition to a serine residue within a consensus sequence of epidermal growth factor epidermal growth factor (EGF)-like repeats found in several proteins, including Notch. Glc provides stability to EGF-like repeats, is required for S2 cleavage of Notch, and serves to regulate the trafficking of Notch, crumbs2, and Eyes shut proteins to the cell surface. Genetic and biochemical studies have shown a link between aberrant protein
O
-glucosylation and human diseases. The main players of protein
O-
glucosylation, protein
O
-glucosyltransferases (POGLUTs), use uridine diphosphate (UDP)-Glc as a substrate to modify EGF repeats and reside in the endoplasmic reticulum via C-terminal KDEL-like signals. In addition to
O
-glucosylation activity, POGLUTs can also perform protein
O
-xylosylation function, i.e., adding xylose (Xyl) from UDP-Xyl; however, both activities rely on residues of EGF repeats, active-site conformations of POGLUTs and sugar substrate concentrations in the ER. Impaired expression of POGLUTs has been associated with initiation and progression of human diseases such as limb-girdle muscular dystrophy, Dowling–Degos disease 4, acute myeloid leukemia, and hepatocytes and pancreatic dysfunction. POGLUTs have been found to alter the expression of cyclin-dependent kinase inhibitors (CDKIs), by affecting Notch or transforming growth factor-β1 signaling, and cause cell proliferation inhibition or induction depending on the particular cell types, which characterizes POGLUT’s cell-dependent dual role. Except for a few downstream elements, the precise mechanisms whereby aberrant protein
O
-glucosylation causes diseases are largely unknown, leaving behind many questions that need to be addressed. This systemic review comprehensively covers literature to understand the
O
-glucosyltransferases with a focus on POGLUT1 structure and function, and their role in health and diseases. Moreover, this study also raises unanswered issues for future research in cancer biology, cell communications, muscular diseases, etc.</description><subject>13</subject><subject>13/1</subject><subject>13/51</subject><subject>13/89</subject><subject>38</subject><subject>38/35</subject><subject>38/70</subject><subject>631/80/458/1524</subject><subject>64</subject><subject>64/24</subject><subject>64/60</subject><subject>692/699/67/395</subject><subject>Acute myeloid leukemia</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell Culture</subject><subject>Cell proliferation</subject><subject>Cell surface</subject><subject>Conserved sequence</subject><subject>Cyclin-dependent kinase</subject><subject>Cyclin-dependent kinase inhibitors</subject><subject>Cyclin-dependent kinases</subject><subject>Endoplasmic reticulum</subject><subject>Epidermal growth factor</subject><subject>Glucosyltransferases - metabolism</subject><subject>Glycosylation</subject><subject>Hepatocytes</subject><subject>Humans</subject><subject>Immunology</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Muscular diseases</subject><subject>Muscular dystrophy</subject><subject>Myeloid leukemia</subject><subject>Oncogenes - physiology</subject><subject>Pancreas</subject><subject>Proteins</subject><subject>Review</subject><subject>Review Article</subject><subject>Serine</subject><subject>Structure-function relationships</subject><subject>Uridine</subject><issn>2041-4889</issn><issn>2041-4889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNp9kU1v1DAQhi0EolXpH-CAInHh0IDHX7EvSKgtUKlSDy1ny3HsNKusvdgOUv492U0pLQd8GcvzzjOeeRF6C_gjYCo_ZQYMVI0JrjGlwOr5BTommEHNpFQvn9yP0GnOG7wcSjHh4jU6opRRwbk8Rhe3JU22TMmdVX4KtgwxnFUmdNXOlPs4xn6uoq92KRY3hOqm7sfJxjyPJZmQvUsmu_wGvfJmzO70IZ6gH18v786_19c3367Ov1zXljNcaseNU60XTduK1krrvRVKSQXQec9BdEQQJoQC6owHq4xvbacaiqmgnW05PUFXK7eLZqN3adiaNOtoBn14iKnXJpXBjk4bgZkirJNcATOcSgLKmkYyQcCC3LM-r6zd1G5dZ11YJhqfQZ9nwnCv-_hLNxLTRpIF8OEBkOLPyeWit0O2bhxNcHHKmrCm4RhLtu_1_h_pJk4pLKs6qLCCBvYqsqpsijkn5x8_A1jvPder53rxXB881_NS9O7pGI8lfxxeBHQV5CUVepf-9v4P9jeiX7ez</recordid><startdate>20210112</startdate><enddate>20210112</enddate><creator>Mehboob, Muhammad Zubair</creator><creator>Lang, Minglin</creator><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Nature Publishing Group</general><scope>C6C</scope><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</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>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-3801-2675</orcidid></search><sort><creationdate>20210112</creationdate><title>Structure, function, and pathology of protein O-glucosyltransferases</title><author>Mehboob, Muhammad Zubair ; Lang, Minglin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c540t-e5ae9bf67bb6bc8cffc6998911dff516d262466913eaf1c9afbcd9730363dcb53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>13</topic><topic>13/1</topic><topic>13/51</topic><topic>13/89</topic><topic>38</topic><topic>38/35</topic><topic>38/70</topic><topic>631/80/458/1524</topic><topic>64</topic><topic>64/24</topic><topic>64/60</topic><topic>692/699/67/395</topic><topic>Acute myeloid leukemia</topic><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Cell Culture</topic><topic>Cell proliferation</topic><topic>Cell surface</topic><topic>Conserved sequence</topic><topic>Cyclin-dependent kinase</topic><topic>Cyclin-dependent kinase inhibitors</topic><topic>Cyclin-dependent kinases</topic><topic>Endoplasmic reticulum</topic><topic>Epidermal growth factor</topic><topic>Glucosyltransferases - metabolism</topic><topic>Glycosylation</topic><topic>Hepatocytes</topic><topic>Humans</topic><topic>Immunology</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>Muscular diseases</topic><topic>Muscular dystrophy</topic><topic>Myeloid leukemia</topic><topic>Oncogenes - physiology</topic><topic>Pancreas</topic><topic>Proteins</topic><topic>Review</topic><topic>Review Article</topic><topic>Serine</topic><topic>Structure-function relationships</topic><topic>Uridine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mehboob, Muhammad Zubair</creatorcontrib><creatorcontrib>Lang, Minglin</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>Cell death & disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mehboob, Muhammad Zubair</au><au>Lang, Minglin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure, function, and pathology of protein O-glucosyltransferases</atitle><jtitle>Cell death & disease</jtitle><stitle>Cell Death Dis</stitle><addtitle>Cell Death Dis</addtitle><date>2021-01-12</date><risdate>2021</risdate><volume>12</volume><issue>1</issue><spage>71</spage><epage>71</epage><pages>71-71</pages><artnum>71</artnum><issn>2041-4889</issn><eissn>2041-4889</eissn><abstract>Protein
O
-glucosylation is a crucial form of
O
-glycosylation, which involves glucose (Glc) addition to a serine residue within a consensus sequence of epidermal growth factor epidermal growth factor (EGF)-like repeats found in several proteins, including Notch. Glc provides stability to EGF-like repeats, is required for S2 cleavage of Notch, and serves to regulate the trafficking of Notch, crumbs2, and Eyes shut proteins to the cell surface. Genetic and biochemical studies have shown a link between aberrant protein
O
-glucosylation and human diseases. The main players of protein
O-
glucosylation, protein
O
-glucosyltransferases (POGLUTs), use uridine diphosphate (UDP)-Glc as a substrate to modify EGF repeats and reside in the endoplasmic reticulum via C-terminal KDEL-like signals. In addition to
O
-glucosylation activity, POGLUTs can also perform protein
O
-xylosylation function, i.e., adding xylose (Xyl) from UDP-Xyl; however, both activities rely on residues of EGF repeats, active-site conformations of POGLUTs and sugar substrate concentrations in the ER. Impaired expression of POGLUTs has been associated with initiation and progression of human diseases such as limb-girdle muscular dystrophy, Dowling–Degos disease 4, acute myeloid leukemia, and hepatocytes and pancreatic dysfunction. POGLUTs have been found to alter the expression of cyclin-dependent kinase inhibitors (CDKIs), by affecting Notch or transforming growth factor-β1 signaling, and cause cell proliferation inhibition or induction depending on the particular cell types, which characterizes POGLUT’s cell-dependent dual role. Except for a few downstream elements, the precise mechanisms whereby aberrant protein
O
-glucosylation causes diseases are largely unknown, leaving behind many questions that need to be addressed. This systemic review comprehensively covers literature to understand the
O
-glucosyltransferases with a focus on POGLUT1 structure and function, and their role in health and diseases. Moreover, this study also raises unanswered issues for future research in cancer biology, cell communications, muscular diseases, etc.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>33436558</pmid><doi>10.1038/s41419-020-03314-y</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-3801-2675</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 13 13/1 13/51 13/89 38 38/35 38/70 631/80/458/1524 64 64/24 64/60 692/699/67/395 Acute myeloid leukemia Antibodies Biochemistry Biomedical and Life Sciences Cell Biology Cell Culture Cell proliferation Cell surface Conserved sequence Cyclin-dependent kinase Cyclin-dependent kinase inhibitors Cyclin-dependent kinases Endoplasmic reticulum Epidermal growth factor Glucosyltransferases - metabolism Glycosylation Hepatocytes Humans Immunology Kinases Life Sciences Muscular diseases Muscular dystrophy Myeloid leukemia Oncogenes - physiology Pancreas Proteins Review Review Article Serine Structure-function relationships Uridine |
title | Structure, function, and pathology of protein O-glucosyltransferases |
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