Multimeric conformation of type III intermediate filaments but not the filamentous conformation exhibits high affinity to lipid bilayers.
Identifieur interne : 000096 ( PubMed/Curation ); précédent : 000095; suivant : 000097Multimeric conformation of type III intermediate filaments but not the filamentous conformation exhibits high affinity to lipid bilayers.
Auteurs : Beomju Hwang [Japon] ; Hirohiko Ise [Japon]Source :
- Genes to cells : devoted to molecular & cellular mechanisms [ 1365-2443 ] ; 2020.
Abstract
Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin, classified as the type III intermediate filament family, maintain the integrity and architecture of various cell types. Recently, we reported their cell surface expression and binding to multivalent N-acetylglucosamine-conjugated polymers. Furthermore, the presence of vimentin on the surface of various cell types including malignant tumor cells and fibroblasts has been demonstrated. Type III intermediate filament proteins are traditionally considered intracellular proteins and do not possess signal peptides for cell membrane recruitment. Therefore, the mechanism of their transport to the cell surface is unclear. In the current study, we aimed to elucidate this mechanism by focusing on the relationship between their multimeric structure and lipid bilayer affinity. Blue native polyacrylamide gel electrophoresis demonstrated that cell surface-expressed type III intermediate filament proteins formed a multimeric mostly including 4-12-mers but not filamentous structure. Moreover, surface plasmon resonance analysis revealed that the multimeric structure of these recombinant proteins had high affinity to lipid bilayers, whereas their filament-like large multimeric structure did not. Our results suggest that type III intermediate filaments are incorporated into the cell membrane through alteration from a filamentous to a multimeric structure.
DOI: 10.1111/gtc.12768
PubMed: 32243065
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Recently, we reported their cell surface expression and binding to multivalent N-acetylglucosamine-conjugated polymers. Furthermore, the presence of vimentin on the surface of various cell types including malignant tumor cells and fibroblasts has been demonstrated. Type III intermediate filament proteins are traditionally considered intracellular proteins and do not possess signal peptides for cell membrane recruitment. Therefore, the mechanism of their transport to the cell surface is unclear. In the current study, we aimed to elucidate this mechanism by focusing on the relationship between their multimeric structure and lipid bilayer affinity. Blue native polyacrylamide gel electrophoresis demonstrated that cell surface-expressed type III intermediate filament proteins formed a multimeric mostly including 4-12-mers but not filamentous structure. Moreover, surface plasmon resonance analysis revealed that the multimeric structure of these recombinant proteins had high affinity to lipid bilayers, whereas their filament-like large multimeric structure did not. Our results suggest that type III intermediate filaments are incorporated into the cell membrane through alteration from a filamentous to a multimeric structure.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32243065</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-2443</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Apr</Month><Day>03</Day></PubDate></JournalIssue><Title>Genes to cells : devoted to molecular & cellular mechanisms</Title><ISOAbbreviation>Genes Cells</ISOAbbreviation></Journal><ArticleTitle>Multimeric conformation of type III intermediate filaments but not the filamentous conformation exhibits high affinity to lipid bilayers.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/gtc.12768</ELocationID><Abstract><AbstractText>Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin, classified as the type III intermediate filament family, maintain the integrity and architecture of various cell types. Recently, we reported their cell surface expression and binding to multivalent N-acetylglucosamine-conjugated polymers. Furthermore, the presence of vimentin on the surface of various cell types including malignant tumor cells and fibroblasts has been demonstrated. Type III intermediate filament proteins are traditionally considered intracellular proteins and do not possess signal peptides for cell membrane recruitment. Therefore, the mechanism of their transport to the cell surface is unclear. In the current study, we aimed to elucidate this mechanism by focusing on the relationship between their multimeric structure and lipid bilayer affinity. Blue native polyacrylamide gel electrophoresis demonstrated that cell surface-expressed type III intermediate filament proteins formed a multimeric mostly including 4-12-mers but not filamentous structure. Moreover, surface plasmon resonance analysis revealed that the multimeric structure of these recombinant proteins had high affinity to lipid bilayers, whereas their filament-like large multimeric structure did not. Our results suggest that type III intermediate filaments are incorporated into the cell membrane through alteration from a filamentous to a multimeric structure.</AbstractText><CopyrightInformation>© 2020 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Beomju</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Graduate School of Engineering, Kyushu University, Fukuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ise</LastName><ForeName>Hirohiko</ForeName><Initials>H</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-4948-9375</Identifier><AffiliationInfo><Affiliation>Institute for Materials Chemistry and Engineering, Kyushu University, Fukuoka, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>KAKENHI JP15K01313</GrantID><Agency>Japan Society for the Promotion of Science</Agency><Country></Country></Grant><Grant><GrantID>KAKENHI JP19K12804</GrantID><Agency>Japan Society for the Promotion of Science</Agency><Country></Country></Grant><Grant><GrantID>the Cooperative Research program of "Network Joi</GrantID><Agency>Ministry of Education, Culture, Sports, Science and Technology</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Genes Cells</MedlineTA><NlmUniqueID>9607379</NlmUniqueID><ISSNLinking>1356-9597</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">GFAP</Keyword><Keyword MajorTopicYN="N">atomic force microscopy</Keyword><Keyword MajorTopicYN="N">cell membrane</Keyword><Keyword MajorTopicYN="N">desmin</Keyword><Keyword MajorTopicYN="N">peripherin</Keyword><Keyword MajorTopicYN="N">surface plasmon resonance</Keyword><Keyword MajorTopicYN="N">type III intermediate filament protein</Keyword><Keyword MajorTopicYN="N">vimentin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>09</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>03</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32243065</ArticleId><ArticleId IdType="doi">10.1111/gtc.12768</ArticleId></ArticleIdList><ReferenceList><Title>REFERENCES</Title><Reference><Citation>Ando, S., Tanabe, K., Gonda, Y., Sato, C., & Inagaki, M. 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