Role for the IFT-A Complex in Selective Transport to the Primary Cilium
Open accessAbstract
Intraflagellar transport sub-complex A (IFT-A) is known to regulate retrograde IFT in the cilium. To rigorously assess its other possible roles, we knocked out an IFT-A subunit, IFT121/WDR35, in mammalian cells and screened the localization of more than 50 proteins. We found that Wdr35 regulates cilium assembly by selectively regulating transport of distinct cargoes. Beyond its role in retrograde transport, we show that Wdr35 functions in fusion of Rab8 vesicles at the nascent cilium, protein exit from the cilium, and centriolar satellite organization. Furthermore, we show that Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits, but the actin network functions to dampen this transport. Wdr35 is mutated in several ciliopathies, and we find that certain disease mutations impair interactions with cargo and other IFT-A subunits. Together, our data link defects in IFT-A mediated cargo transport with disease.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The IFT-A complex interacts with the tubby domain proteins TULP3 and TUB to mediate ciliary targeting of certain transmembrane proteins, including G protein-coupled receptors.
“Furthermore, the IFT-A complex interacts with the tubby domain proteins TULP3 and TUB to mediate ciliary targeting of certain transmembrane proteins, including G protein-coupled receptors (GPCRs) 56, 58, 64–69.”
From Cellular signalling by primary cilia in development, organ function and disease (2019) · cites this paper as [68]
The Results section, “Integrated function of Wdr35-IFT-A complex” (page unavailable), reports interactions between IFT-A subunits and ciliary membrane cargoes, including the GPCR SSTR3, supporting a role in cargo transport. Our copy does not report interactions with TULP3 or TUB; TULP3 appears in the title of a work listed in the References, but that does not establish the claimed interactions for this paper. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
The citation lists haven’t been fetched yet
References 64 · Cited by 86
- Authors
- Fu, W., Wang, L., Kim, S., Li, J., & Dynlacht, B. D.
- Affiliations
- NYU Langone’s Laura and Isaac Perlmutter Cancer Center (US)
- Broad Institute (US)
- Corresponding author
- Dynlacht, Brian David
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 17
- Issue
- 6
- Pages
- 1505-1517
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC5123888
- OpenAlex
- W2548338156
- Cited by
- 86
- References
- 64
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 10 · 2021: 12 · 2020: 4 · 2019: 14 · 2018: 16 · 2017: 12 · 2015: 1
- FWCI
- 11.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- NIH (HD069647, R01 GM 120776-05A1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Cystic Fibrosis Research Advances
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Keywords
- IFT-A complex, intraflagellar transport, primary cilia, retrograde transport, centriolar satellites, actin networks, ciliopathies, freight transport, subcellular protein localization
- MeSH terms
- Actins, Cell Line, Centrioles, Cilia, Cytoskeletal Proteins, Humans, Actin Cytoskeleton, Models, Biological, Mutation, Proteins, Cytochalasin D, Centrosome, Protein Subunits, Protein Transport, Organogenesis, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Hedgehog Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
