PittsburghV1, PubMed, Checkpoint, bibRecord, 002934

IFT27 links the BBSome to IFT for maintenance of the ciliary signaling compartment.

Identifieur interne : 002934 ( PubMed/Checkpoint ); précédent : 002933; suivant : 002935

IFT27 links the BBSome to IFT for maintenance of the ciliary signaling compartment.

Auteurs : Thibaut Eguether [États-Unis] ; Jovenal T. San Agustin [États-Unis] ; Brian T. Keady [États-Unis] ; Julie A. Jonassen [États-Unis] ; Yinwen Liang [République populaire de Chine] ; Richard Francis [États-Unis] ; Kimimasa Tobita [États-Unis] ; Colin A. Johnson [Royaume-Uni] ; Zakia A. Abdelhamed [Royaume-Uni] ; Cecilia W. Lo [États-Unis] ; Gregory J. Pazour [États-Unis]

Source :

Developmental cell [ 1878-1551 ] ; 2014.

RBID : pubmed:25446516

Descripteurs français

English descriptors

KwdEn :
- Animals, Biological Transport, Cilia (metabolism), Flagella (metabolism), Hedgehog Proteins (metabolism), Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Receptors, Cell Surface (metabolism), Signal Transduction, Transcription Factors (metabolism), rab GTP-Binding Proteins (metabolism).
MESH :
- chemical , metabolism : Hedgehog Proteins, Receptors, Cell Surface, Transcription Factors, rab GTP-Binding Proteins.
- metabolism : Cilia, Flagella.
- Animals, Biological Transport, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Signal Transduction.

Abstract

Vertebrate hedgehog signaling is coordinated by the differential localization of the receptors patched-1 and Smoothened in the primary cilium. Cilia assembly is mediated by intraflagellar transport (IFT), and cilia defects disrupt hedgehog signaling, causing many structural birth defects. We generated Ift25 and Ift27 knockout mice and show that they have structural birth defects indicative of hedgehog signaling dysfunction. Surprisingly, ciliary assembly is not affected, but abnormal hedgehog signaling is observed in conjunction with ciliary accumulation of patched-1 and Smoothened. Similarly, Smoothened accumulates in cilia on cells mutated for BBSome components or the BBS binding protein/regulator Lztfl1. Interestingly, the BBSome and Lztfl1 accumulate to high levels in Ift27 mutant cilia. Because Lztfl1 mutant cells accumulate BBSome but not IFT27, it is likely that Lztfl1 functions downstream of IFT27 to couple the BBSome to the IFT particle for coordinated removal of patched-1 and Smoothened from cilia during hedgehog signaling.

DOI: 10.1016/j.devcel.2014.09.011
PubMed: 25446516

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Biological Transport</term>
<term>Cilia (metabolism)</term>
<term>Flagella (metabolism)</term>
<term>Hedgehog Proteins (metabolism)</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Mice, Knockout</term>
<term>Mice, Transgenic</term>
<term>Receptors, Cell Surface (metabolism)</term>
<term>Signal Transduction</term>
<term>Transcription Factors (metabolism)</term>
<term>rab GTP-Binding Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cils vibratiles (métabolisme)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Flagelles (métabolisme)</term>
<term>Protéines G rab (métabolisme)</term>
<term>Protéines Hedgehog (métabolisme)</term>
<term>Récepteurs de surface cellulaire (métabolisme)</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
<term>Souris knockout</term>
<term>Souris transgéniques</term>
<term>Transduction du signal</term>
<term>Transport biologique</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hedgehog Proteins</term>
<term>Receptors, Cell Surface</term>
<term>Transcription Factors</term>
<term>rab GTP-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cilia</term>
<term>Flagella</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cils vibratiles</term>
<term>Facteurs de transcription</term>
<term>Flagelles</term>
<term>Protéines G rab</term>
<term>Protéines Hedgehog</term>
<term>Récepteurs de surface cellulaire</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Biological Transport</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Mice, Knockout</term>
<term>Mice, Transgenic</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
<term>Souris knockout</term>
<term>Souris transgéniques</term>
<term>Transduction du signal</term>
<term>Transport biologique</term>
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<front><div type="abstract" xml:lang="en">Vertebrate hedgehog signaling is coordinated by the differential localization of the receptors patched-1 and Smoothened in the primary cilium. Cilia assembly is mediated by intraflagellar transport (IFT), and cilia defects disrupt hedgehog signaling, causing many structural birth defects. We generated Ift25 and Ift27 knockout mice and show that they have structural birth defects indicative of hedgehog signaling dysfunction. Surprisingly, ciliary assembly is not affected, but abnormal hedgehog signaling is observed in conjunction with ciliary accumulation of patched-1 and Smoothened. Similarly, Smoothened accumulates in cilia on cells mutated for BBSome components or the BBS binding protein/regulator Lztfl1. Interestingly, the BBSome and Lztfl1 accumulate to high levels in Ift27 mutant cilia. Because Lztfl1 mutant cells accumulate BBSome but not IFT27, it is likely that Lztfl1 functions downstream of IFT27 to couple the BBSome to the IFT particle for coordinated removal of patched-1 and Smoothened from cilia during hedgehog signaling.</div>
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<Abstract><AbstractText>Vertebrate hedgehog signaling is coordinated by the differential localization of the receptors patched-1 and Smoothened in the primary cilium. Cilia assembly is mediated by intraflagellar transport (IFT), and cilia defects disrupt hedgehog signaling, causing many structural birth defects. We generated Ift25 and Ift27 knockout mice and show that they have structural birth defects indicative of hedgehog signaling dysfunction. Surprisingly, ciliary assembly is not affected, but abnormal hedgehog signaling is observed in conjunction with ciliary accumulation of patched-1 and Smoothened. Similarly, Smoothened accumulates in cilia on cells mutated for BBSome components or the BBS binding protein/regulator Lztfl1. Interestingly, the BBSome and Lztfl1 accumulate to high levels in Ift27 mutant cilia. Because Lztfl1 mutant cells accumulate BBSome but not IFT27, it is likely that Lztfl1 functions downstream of IFT27 to couple the BBSome to the IFT particle for coordinated removal of patched-1 and Smoothened from cilia during hedgehog signaling.</AbstractText>
<CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Eguether</LastName>
<ForeName>Thibaut</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Program in Molecular Medicine, University of Massachusetts Medical School, Biotech II, Suite 213, 373 Plantation Street, Worcester, MA 01605, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>San Agustin</LastName>
<ForeName>Jovenal T</ForeName>
<Initials>JT</Initials>
<AffiliationInfo><Affiliation>Program in Molecular Medicine, University of Massachusetts Medical School, Biotech II, Suite 213, 373 Plantation Street, Worcester, MA 01605, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Keady</LastName>
<ForeName>Brian T</ForeName>
<Initials>BT</Initials>
<AffiliationInfo><Affiliation>Program in Molecular Medicine, University of Massachusetts Medical School, Biotech II, Suite 213, 373 Plantation Street, Worcester, MA 01605, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jonassen</LastName>
<ForeName>Julie A</ForeName>
<Initials>JA</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liang</LastName>
<ForeName>Yinwen</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Program in Molecular Medicine, University of Massachusetts Medical School, Biotech II, Suite 213, 373 Plantation Street, Worcester, MA 01605, USA; School of Life Sciences, Tsinghua University, Renhuan Lou 413, #1 Qinghuayuan, Haidian District, Beijing 100084, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Francis</LastName>
<ForeName>Richard</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Developmental Biology, University of Pittsburgh, 8111 Rangos Research Center, 530 45th Street, Pittsburgh, PA 15201, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tobita</LastName>
<ForeName>Kimimasa</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Developmental Biology, University of Pittsburgh, 8111 Rangos Research Center, 530 45th Street, Pittsburgh, PA 15201, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Colin A</ForeName>
<Initials>CA</Initials>
<AffiliationInfo><Affiliation>Section of Ophthalmology and Neurosciences, Wellcome Trust Brenner Building, Leeds Institute of Molecular Medicine, University of Leeds, St. James's University Hospital, Beckett Street, Leeds LS9 7TF, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Abdelhamed</LastName>
<ForeName>Zakia A</ForeName>
<Initials>ZA</Initials>
<AffiliationInfo><Affiliation>Section of Ophthalmology and Neurosciences, Wellcome Trust Brenner Building, Leeds Institute of Molecular Medicine, University of Leeds, St. James's University Hospital, Beckett Street, Leeds LS9 7TF, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lo</LastName>
<ForeName>Cecilia W</ForeName>
<Initials>CW</Initials>
<AffiliationInfo><Affiliation>Department of Developmental Biology, University of Pittsburgh, 8111 Rangos Research Center, 530 45th Street, Pittsburgh, PA 15201, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pazour</LastName>
<ForeName>Gregory J</ForeName>
<Initials>GJ</Initials>
<AffiliationInfo><Affiliation>Program in Molecular Medicine, University of Massachusetts Medical School, Biotech II, Suite 213, 373 Plantation Street, Worcester, MA 01605, USA. Electronic address: gregory.pazour@umassmed.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>GM060992</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>DK074038</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>G0700073</GrantID>
<Agency>Medical Research Council</Agency>
<Country>United Kingdom</Country>
</Grant>
<Grant><GrantID>P30 DK074038</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>5U01HL098180</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P30 DK032520</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>DK32520</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>U01 HL098180</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 GM060992</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>10</Month>
<Day>30</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Dev Cell</MedlineTA>
<NlmUniqueID>101120028</NlmUniqueID>
<ISSNLinking>1534-5807</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D053823">Hedgehog Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C486612">Lztfl1protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011956">Receptors, Cell Surface</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000595889">intraflagellar transport 27 protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber>
<NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002923" MajorTopicYN="N">Cilia</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005407" MajorTopicYN="N">Flagella</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053823" MajorTopicYN="N">Hedgehog Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018345" MajorTopicYN="N">Mice, Knockout</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008822" MajorTopicYN="N">Mice, Transgenic</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011956" MajorTopicYN="N">Receptors, Cell Surface</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<OtherID Source="NLM">NIHMS631466</OtherID>
<OtherID Source="NLM">PMC4254547</OtherID>
</MedlineCitation>
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<Month>06</Month>
<Day>11</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2014</Year>
<Month>09</Month>
<Day>12</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2014</Year>
<Month>09</Month>
<Day>23</Day>
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<ArticleIdList><ArticleId IdType="pubmed">25446516</ArticleId>
<ArticleId IdType="pii">S1534-5807(14)00617-0</ArticleId>
<ArticleId IdType="doi">10.1016/j.devcel.2014.09.011</ArticleId>
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<affiliations><list><country><li>Royaume-Uni</li>
<li>République populaire de Chine</li>
<li>États-Unis</li>
</country>
<region><li>Angleterre</li>
<li>Massachusetts</li>
<li>Pennsylvanie</li>
<li>Yorkshire-et-Humber</li>
</region>
<settlement><li>Leeds</li>
<li>Pittsburgh</li>
<li>Pékin</li>
</settlement>
<orgName><li>Université de Leeds</li>
<li>Université de Pittsburgh</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Eguether, Thibaut" sort="Eguether, Thibaut" uniqKey="Eguether T" first="Thibaut" last="Eguether">Thibaut Eguether</name>
</region>
<name sortKey="Francis, Richard" sort="Francis, Richard" uniqKey="Francis R" first="Richard" last="Francis">Richard Francis</name>
<name sortKey="Jonassen, Julie A" sort="Jonassen, Julie A" uniqKey="Jonassen J" first="Julie A" last="Jonassen">Julie A. Jonassen</name>
<name sortKey="Keady, Brian T" sort="Keady, Brian T" uniqKey="Keady B" first="Brian T" last="Keady">Brian T. Keady</name>
<name sortKey="Lo, Cecilia W" sort="Lo, Cecilia W" uniqKey="Lo C" first="Cecilia W" last="Lo">Cecilia W. Lo</name>
<name sortKey="Pazour, Gregory J" sort="Pazour, Gregory J" uniqKey="Pazour G" first="Gregory J" last="Pazour">Gregory J. Pazour</name>
<name sortKey="San Agustin, Jovenal T" sort="San Agustin, Jovenal T" uniqKey="San Agustin J" first="Jovenal T" last="San Agustin">Jovenal T. San Agustin</name>
<name sortKey="Tobita, Kimimasa" sort="Tobita, Kimimasa" uniqKey="Tobita K" first="Kimimasa" last="Tobita">Kimimasa Tobita</name>
</country>
<country name="République populaire de Chine"><noRegion><name sortKey="Liang, Yinwen" sort="Liang, Yinwen" uniqKey="Liang Y" first="Yinwen" last="Liang">Yinwen Liang</name>
</noRegion>
</country>
<country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Johnson, Colin A" sort="Johnson, Colin A" uniqKey="Johnson C" first="Colin A" last="Johnson">Colin A. Johnson</name>
</region>
<name sortKey="Abdelhamed, Zakia A" sort="Abdelhamed, Zakia A" uniqKey="Abdelhamed Z" first="Zakia A" last="Abdelhamed">Zakia A. Abdelhamed</name>
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IFT27 links the BBSome to IFT for maintenance of the ciliary signaling compartment.

IFT27 links the BBSome to IFT for maintenance of the ciliary signaling compartment.

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