Evidence map›Paper›PMID 40571631›Full record

ArticleCell structure and function2025

Assembly and mother centriole recruitment of IFT-B subcomplexes to form IFT-B holocomplex.

Koshi Tasaki, Yohei Katoh, Hye-Won Shin, Kazuhisa Nakayama

Abstract read
In one paragraph

Article in Cell structure and function, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Koshi TasakiDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University.
Yohei KatohDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University.ORCID http://orcid.org/0000-0003-1649-4917
Hye-Won ShinDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University.ORCID http://orcid.org/0000-0002-9138-9554
Kazuhisa NakayamaDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University.ORCID http://orcid.org/0000-0001-7701-7183

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the biogenesis and maintenance of cilia, bidirectional protein trafficking within cilia is crucial, and is conducted by intraflagellar transport (IFT) trains containing the IFT-A and IFT-B complexes that are powered by dynein-2 and kinesin-II motors. We have recently shown that before the assembly of anterograde IFT trains, the IFT-A, IFT-B, and dynein-2 complexes are independently recruited to the mother centriole/basal body. The IFT-B complex, which consists of 16 subunits, can be divided into the IFT-B1 and IFT-B2 subcomplexes, and IFT-B1 can be further divided into the IFT-B1a and IFT-B1b subgroups. Here we investigated how the IFT-B complex is assembled and recruited to the mother centriole for ciliogenesis. Analyses using cells with knockouts of individual IFT-B subunits, and analyses of proteins coimmunoprecipitated with EGFP-fused IFT-B2, IFT-B1b, and IFT-B1a subunits expressed in these knockout cells demonstrated the following: (i) although IFT-B2 is dispensable for the linkage between IFT-B1b and IFT-B1a, it is essential for their localization to the mother centriole; (ii) IFT-B1b is essential both for bridging IFT-B2 and IFT-B1a, and for their localization to the mother centriole; (iii) IFT-B1a is not required for the linkage between IFT-B2 and IFT-B1b nor for their localization to the mother centriole; and (iv) all IFT-B components (IFT-B2, IFT-B1b, and IFT-B1a) are essential for ciliogenesis. Thus, although ciliogenesis is not a prerequisite for the recruitment of the IFT-B complex to the mother centriole, the linkage between IFT-B2 and IFT-B1b is crucial for the mother centriole localization of the IFT-B complex for ciliogenesis.Key words: cilia, ciliogenesis, distal appendages, IFT-B complex, mother centriole.

Indexed as

CentriolesCiliaAnimalsHumansProtein Transportciliaciliogenesisdistal appendagesIFT-B complexmother centriole

Identifiers

PMID40571631
PMCPMC12967509

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