WSB1: from homeostasis to hypoxia.
Identifieur interne : 000182 ( PubMed/Curation ); précédent : 000181; suivant : 000183WSB1: from homeostasis to hypoxia.
Auteurs : Moinul Haque [Canada] ; Joseph Keith Kendal [Canada] ; Ryan Matthew Macisaac [Canada] ; Douglas James Demetrick [Canada]Source :
- Journal of biomedical science [ 1423-0127 ] ; 2016.
English descriptors
- KwdEn :
- Animals, Homeostasis, Humans, Hypoxia (metabolism), Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (metabolism), Neoplasm Proteins (metabolism), Neoplasms (metabolism), Neoplasms (pathology), Parkinson Disease (metabolism), Parkinson Disease (pathology), Proteins (metabolism), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
- MESH :
- chemical , metabolism : Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Neoplasm Proteins, Proteins, Ubiquitin-Protein Ligases.
- metabolism : Hypoxia, Neoplasms, Parkinson Disease.
- pathology : Neoplasms, Parkinson Disease.
- Animals, Homeostasis, Humans, Ubiquitination.
Abstract
The wsb1 gene has been identified to be important in developmental biology and cancer. A complex transcriptional regulation of wsb1 yields at least three functional transcripts. The major expressed isoform, WSB1 protein, is a substrate recognition protein within an E3 ubiquitin ligase, with the capability to bind diverse targets and mediate ubiquitinylation and proteolytic degradation. Recent data suggests a new role for WSB1 as a component of a neuroprotective pathway which results in modification and aggregation of neurotoxic proteins such as LRRK2 in Parkinson's Disease, via an unusual mode of protein ubiquitinylation.WSB1 is also involved in thyroid hormone homeostasis, immune regulation and cellular metabolism, particularly glucose metabolism and hypoxia. In hypoxia, wsb1 is a HIF-1 target, and is a regulator of the degradation of diverse proteins associated with the cellular response to hypoxia, including HIPK2, RhoGDI2 and VHL. Major roles are to both protect HIF-1 function through degradation of VHL, and decrease apoptosis through degradation of HIPK2. These activities suggest a role for wsb1 in cancer cell proliferation and metastasis. As well, recent work has identified a role for WSB1 in glucose metabolism, and perhaps in mediating the Warburg effect in cancer cells by maintaining the function of HIF1. Furthermore, studies of cancer specimens have identified dysregulation of wsb1 associated with several types of cancer, suggesting a biologically relevant role in cancer development and/or progression.Recent development of an inducible expression system for wsb1 could aid in the further understanding of the varied functions of this protein in the cell, and roles as a potential oncogene and neuroprotective protein.
DOI: 10.1186/s12929-016-0270-3
PubMed: 27542736
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pubmed:27542736Le document en format XML
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Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1</wicri:regionArea></affiliation></author><author><name sortKey="Kendal, Joseph Keith" sort="Kendal, Joseph Keith" uniqKey="Kendal J" first="Joseph Keith" last="Kendal">Joseph Keith Kendal</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1</wicri:regionArea></affiliation></author><author><name sortKey="Macisaac, Ryan Matthew" sort="Macisaac, Ryan Matthew" uniqKey="Macisaac R" first="Ryan Matthew" last="Macisaac">Ryan Matthew Macisaac</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1</wicri:regionArea></affiliation></author><author><name sortKey="Demetrick, Douglas James" sort="Demetrick, Douglas James" uniqKey="Demetrick D" first="Douglas James" last="Demetrick">Douglas James Demetrick</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada. demetric@ucalgary.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1</wicri:regionArea></affiliation></author></analytic><series><title level="j">Journal of biomedical science</title><idno type="eISSN">1423-0127</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Homeostasis</term><term>Humans</term><term>Hypoxia (metabolism)</term><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 (metabolism)</term><term>Neoplasm Proteins (metabolism)</term><term>Neoplasms (metabolism)</term><term>Neoplasms (pathology)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>Proteins (metabolism)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2</term><term>Neoplasm Proteins</term><term>Proteins</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Hypoxia</term><term>Neoplasms</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neoplasms</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Homeostasis</term><term>Humans</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The wsb1 gene has been identified to be important in developmental biology and cancer. A complex transcriptional regulation of wsb1 yields at least three functional transcripts. The major expressed isoform, WSB1 protein, is a substrate recognition protein within an E3 ubiquitin ligase, with the capability to bind diverse targets and mediate ubiquitinylation and proteolytic degradation. Recent data suggests a new role for WSB1 as a component of a neuroprotective pathway which results in modification and aggregation of neurotoxic proteins such as LRRK2 in Parkinson's Disease, via an unusual mode of protein ubiquitinylation.WSB1 is also involved in thyroid hormone homeostasis, immune regulation and cellular metabolism, particularly glucose metabolism and hypoxia. In hypoxia, wsb1 is a HIF-1 target, and is a regulator of the degradation of diverse proteins associated with the cellular response to hypoxia, including HIPK2, RhoGDI2 and VHL. Major roles are to both protect HIF-1 function through degradation of VHL, and decrease apoptosis through degradation of HIPK2. These activities suggest a role for wsb1 in cancer cell proliferation and metastasis. As well, recent work has identified a role for WSB1 in glucose metabolism, and perhaps in mediating the Warburg effect in cancer cells by maintaining the function of HIF1. Furthermore, studies of cancer specimens have identified dysregulation of wsb1 associated with several types of cancer, suggesting a biologically relevant role in cancer development and/or progression.Recent development of an inducible expression system for wsb1 could aid in the further understanding of the varied functions of this protein in the cell, and roles as a potential oncogene and neuroprotective protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27542736</PMID><DateCreated><Year>2016</Year><Month>08</Month><Day>20</Day></DateCreated><DateCompleted><Year>2017</Year><Month>02</Month><Day>01</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1423-0127</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>1</Issue><PubDate><Year>2016</Year><Month>Aug</Month><Day>19</Day></PubDate></JournalIssue><Title>Journal of biomedical science</Title><ISOAbbreviation>J. Biomed. Sci.</ISOAbbreviation></Journal><ArticleTitle>WSB1: from homeostasis to hypoxia.</ArticleTitle><Pagination><MedlinePgn>61</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/s12929-016-0270-3</ELocationID><Abstract><AbstractText>The wsb1 gene has been identified to be important in developmental biology and cancer. A complex transcriptional regulation of wsb1 yields at least three functional transcripts. The major expressed isoform, WSB1 protein, is a substrate recognition protein within an E3 ubiquitin ligase, with the capability to bind diverse targets and mediate ubiquitinylation and proteolytic degradation. Recent data suggests a new role for WSB1 as a component of a neuroprotective pathway which results in modification and aggregation of neurotoxic proteins such as LRRK2 in Parkinson's Disease, via an unusual mode of protein ubiquitinylation.WSB1 is also involved in thyroid hormone homeostasis, immune regulation and cellular metabolism, particularly glucose metabolism and hypoxia. In hypoxia, wsb1 is a HIF-1 target, and is a regulator of the degradation of diverse proteins associated with the cellular response to hypoxia, including HIPK2, RhoGDI2 and VHL. Major roles are to both protect HIF-1 function through degradation of VHL, and decrease apoptosis through degradation of HIPK2. These activities suggest a role for wsb1 in cancer cell proliferation and metastasis. As well, recent work has identified a role for WSB1 in glucose metabolism, and perhaps in mediating the Warburg effect in cancer cells by maintaining the function of HIF1. Furthermore, studies of cancer specimens have identified dysregulation of wsb1 associated with several types of cancer, suggesting a biologically relevant role in cancer development and/or progression.Recent development of an inducible expression system for wsb1 could aid in the further understanding of the varied functions of this protein in the cell, and roles as a potential oncogene and neuroprotective protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Haque</LastName><ForeName>Moinul</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Oncology, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Medical Biochemistry, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kendal</LastName><ForeName>Joseph Keith</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Oncology, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Medical Biochemistry, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>MacIsaac</LastName><ForeName>Ryan Matthew</ForeName><Initials>RM</Initials><AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Oncology, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Medical Biochemistry, University of Calgary, Calgary, AB, T2N 4N1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Demetrick</LastName><ForeName>Douglas James</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Department of Pathology and Laboratory Medicine, University of Calgary, Calgary, AB, T2N 4N1, Canada. demetric@ucalgary.ca.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Oncology, University of Calgary, Calgary, AB, T2N 4N1, Canada. demetric@ucalgary.ca.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Medical Biochemistry, University of Calgary, Calgary, AB, T2N 4N1, Canada. demetric@ucalgary.ca.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Calgary Laboratory Services, Room 302, HMRB, 3330 Hospital Dr. N.W., Calgary, AB, T2N 4N1, Canada. demetric@ucalgary.ca.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Biomed Sci</MedlineTA><NlmUniqueID>9421567</NlmUniqueID><ISSNLinking>1021-7770</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009363">Neoplasm Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C120287">WSB1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance 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Kinase-2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009363" MajorTopicYN="N">Neoplasm Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009369" MajorTopicYN="N">Neoplasms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054875" MajorTopicYN="N">Ubiquitination</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4992216</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cancer</Keyword><Keyword MajorTopicYN="N">E3 ubiquitin ligase</Keyword><Keyword MajorTopicYN="N">HIPK2</Keyword><Keyword MajorTopicYN="N">Hypoxia</Keyword><Keyword MajorTopicYN="N">VHL</Keyword><Keyword MajorTopicYN="N">WSB1</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>03</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>07</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>8</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>8</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>2</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27542736</ArticleId><ArticleId IdType="doi">10.1186/s12929-016-0270-3</ArticleId><ArticleId IdType="pii">10.1186/s12929-016-0270-3</ArticleId><ArticleId IdType="pmc">PMC4992216</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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