Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis
Intraflagellar transport (IFT) particles or trains are composed of IFT-A and IFT-B complexes. To assess the working mechanism of the IFT-A complex in IFT and ciliogenesis, we have analyzed ift43 mutants of Chlamydomnonas in conjunction with mutants of the other IFT-A subunits. An ift43 null mutant o...
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| creator | Zhu, Bing Zhu, Xin Wang, Limei Liang, Yinwen Feng, Qianqian Pan, Junmin |
| description | Intraflagellar transport (IFT) particles or trains are composed of IFT-A and IFT-B complexes. To assess the working mechanism of the IFT-A complex in IFT and ciliogenesis, we have analyzed ift43 mutants of Chlamydomnonas in conjunction with mutants of the other IFT-A subunits. An ift43 null mutant or a mutant with a partial deletion of the IFT43 conserved domain has no or short flagella. The mutants accumulate not only IFT-B but also IFT-Ain the short flagella, which is in contrast to an ift140 null mutant. The IFT43 conserved domain is necessary and sufficient for the function of IFT43. IFT43 directly interacts with IFT121 and loss of IFT43 results in instability of IFT-A. A construct with a partial deletion of the IFT43 conserved domain is sufficient to rescue the instability phenotype of IFT-A, but results in diminishing of IFT-A at the peri-basal body region. We have further provided evidence for the direct interactions within the IFT-A complex and shown that the integrity of IFT-A is important for its stability and cellular localization. Finally, we show that both IFT43 and IFT140 are involved in mobilizing ciliary precursors from the cytoplasmic pool during flagellar regeneration, suggesting a novel role of IFT-A in transporting ciliary components in the cytoplasm to the peri-basal body region. |
| doi_str_mv | 10.1371/journal.pgen.1006627 |
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To assess the working mechanism of the IFT-A complex in IFT and ciliogenesis, we have analyzed ift43 mutants of Chlamydomnonas in conjunction with mutants of the other IFT-A subunits. An ift43 null mutant or a mutant with a partial deletion of the IFT43 conserved domain has no or short flagella. The mutants accumulate not only IFT-B but also IFT-Ain the short flagella, which is in contrast to an ift140 null mutant. The IFT43 conserved domain is necessary and sufficient for the function of IFT43. IFT43 directly interacts with IFT121 and loss of IFT43 results in instability of IFT-A. A construct with a partial deletion of the IFT43 conserved domain is sufficient to rescue the instability phenotype of IFT-A, but results in diminishing of IFT-A at the peri-basal body region. We have further provided evidence for the direct interactions within the IFT-A complex and shown that the integrity of IFT-A is important for its stability and cellular localization. Finally, we show that both IFT43 and IFT140 are involved in mobilizing ciliary precursors from the cytoplasmic pool during flagellar regeneration, suggesting a novel role of IFT-A in transporting ciliary components in the cytoplasm to the peri-basal body region.</description><identifier>ISSN: 1553-7404</identifier><identifier>ISSN: 1553-7390</identifier><identifier>EISSN: 1553-7404</identifier><identifier>DOI: 10.1371/journal.pgen.1006627</identifier><identifier>PMID: 28207750</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Algal Proteins - genetics ; Analysis ; Biological Transport - genetics ; Biology and Life Sciences ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell cycle ; Chlamydomonas reinhardtii - genetics ; Chlamydomonas reinhardtii - metabolism ; Cilia - genetics ; Cytogenetics ; Cytoplasm - genetics ; Deoxyribonucleic acid ; DNA ; Flagella - genetics ; Flagella - metabolism ; Funding ; Genes ; Immunoglobulins ; Laboratories ; Life sciences ; Localization ; Medicine and Health Sciences ; Multiprotein Complexes - genetics ; Phenotype ; Protein Binding ; Proteins ; Research and Analysis Methods ; Sequence Deletion</subject><ispartof>PLoS genetics, 2017-02, Vol.13 (2), p.e1006627-e1006627</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Zhu B, Zhu X, Wang L, Liang Y, Feng Q, Pan J (2017) Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis. PLoS Genet 13(2): e1006627. doi:10.1371/journal.pgen.1006627</rights><rights>2017 Zhu et al 2017 Zhu et al</rights><rights>2017 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Zhu B, Zhu X, Wang L, Liang Y, Feng Q, Pan J (2017) Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Bing</au><au>Zhu, Xin</au><au>Wang, Limei</au><au>Liang, Yinwen</au><au>Feng, Qianqian</au><au>Pan, Junmin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis</atitle><jtitle>PLoS genetics</jtitle><addtitle>PLoS Genet</addtitle><date>2017-02-16</date><risdate>2017</risdate><volume>13</volume><issue>2</issue><spage>e1006627</spage><epage>e1006627</epage><pages>e1006627-e1006627</pages><issn>1553-7404</issn><issn>1553-7390</issn><eissn>1553-7404</eissn><abstract>Intraflagellar transport (IFT) particles or trains are composed of IFT-A and IFT-B complexes. To assess the working mechanism of the IFT-A complex in IFT and ciliogenesis, we have analyzed ift43 mutants of Chlamydomnonas in conjunction with mutants of the other IFT-A subunits. An ift43 null mutant or a mutant with a partial deletion of the IFT43 conserved domain has no or short flagella. The mutants accumulate not only IFT-B but also IFT-Ain the short flagella, which is in contrast to an ift140 null mutant. The IFT43 conserved domain is necessary and sufficient for the function of IFT43. IFT43 directly interacts with IFT121 and loss of IFT43 results in instability of IFT-A. A construct with a partial deletion of the IFT43 conserved domain is sufficient to rescue the instability phenotype of IFT-A, but results in diminishing of IFT-A at the peri-basal body region. We have further provided evidence for the direct interactions within the IFT-A complex and shown that the integrity of IFT-A is important for its stability and cellular localization. Finally, we show that both IFT43 and IFT140 are involved in mobilizing ciliary precursors from the cytoplasmic pool during flagellar regeneration, suggesting a novel role of IFT-A in transporting ciliary components in the cytoplasm to the peri-basal body region.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28207750</pmid><doi>10.1371/journal.pgen.1006627</doi><orcidid>https://orcid.org/0000-0003-1242-3791</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Algal Proteins - genetics Analysis Biological Transport - genetics Biology and Life Sciences Carrier Proteins - genetics Carrier Proteins - metabolism Cell cycle Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism Cilia - genetics Cytogenetics Cytoplasm - genetics Deoxyribonucleic acid DNA Flagella - genetics Flagella - metabolism Funding Genes Immunoglobulins Laboratories Life sciences Localization Medicine and Health Sciences Multiprotein Complexes - genetics Phenotype Protein Binding Proteins Research and Analysis Methods Sequence Deletion |
| title | Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis |
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