ArticleCurrent biology : CB2014
An assay for clogging the ciliary pore complex distinguishes mechanisms of cytosolic and membrane protein entry.
Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 54 citations in OpenAlex.
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Article
- Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies.Nature reviews. Nephrology · 2024Review
- Monitoring HIV-1 Nuclear Import Kinetics Using a Chemically Induced Nuclear Pore Blockade Assay.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Deciphering vesicle-assisted transport mechanisms in cytoplasm to cilium trafficking.Frontiers in cellular neuroscience · 2024Review
- Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023Review
- Composition, organization and mechanisms of the transition zone, a gate for the cilium.EMBO reports · 2022Review
- Structure and dynamics of photoreceptor sensory cilia.Pflugers Archiv : European journal of physiology · 2021Review
- Interactions of HIV-1 Capsid with Host Factors and Their Implications for Developing Novel Therapeutics.Viruses · 2021Review
- Early HIV replication revisited.Nature microbiology · 2020Article
- Nuclear pore blockade reveals that HIV-1 completes reverse transcription and uncoating in the nucleus.Nature microbiology · 2020Article
- Acute Inhibition of Heterotrimeric Kinesin-2 Function Reveals Mechanisms of Intraflagellar Transport in Mammalian Cilia.Current biology : CB · 2019Article
- Review
- NPHP proteins are binding partners of nucleoporins at the base of the primary cilium.PloS one · 2019Article
- RPGRIP1L helps to establish the ciliary gate for entry of proteins.Journal of cell science · 2018Article
- NUP98 Sets the Size-Exclusion Diffusion Limit through the Ciliary Base.Current biology : CB · 2018Article
- Mechanisms of ciliary targeting: entering importins and Rabs.Cellular and molecular life sciences : CMLS · 2018Review
- Protein Interaction Analysis Provides a Map of the Spatial and Temporal Organization of the Ciliary Gating Zone.Current biology : CB · 2017Article
- Arl3 and RP2 regulate the trafficking of ciliary tip kinesins.Human molecular genetics · 2017Article
- Tubby family proteins are adapters for ciliary trafficking of integral membrane proteins.The Journal of cell biology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
As a cellular organelle, the cilium contains a unique protein composition. Entry of both membrane and cytosolic components is tightly regulated by gating mechanisms at the cilium base; however, the mechanistic details of ciliary gating are largely unknown. We previously proposed that entry of cytosolic components is regulated by mechanisms similar to those of nuclear transport and is dependent on nucleoporins (NUPs), which comprise a ciliary pore complex (CPC). To investigate ciliary gating mechanisms, we developed a system to clog the pore by inhibiting NUP function via forced dimerization. We targeted NUP62, a component of the central channel of the nuclear pore complex (NPC), for forced dimerization by tagging it with the homodimerizing Fv domain. As proof of principle, we show that forced dimerization of NUP62-Fv attenuated (1) active transport of BSA into the nuclear compartment and (2) the kinesin-2 motor KIF17 into the ciliary compartment. Using the pore-clogging technique, we find that forced dimerization of NUP62 attenuated the gated entry of cytosolic proteins but did not affect entry of membrane proteins or diffusional entry of small cytosolic proteins. We propose a model in which active transport of cytosolic proteins into both nuclear and ciliary compartments requires functional NUPs of the central pore, whereas lateral entry of membrane proteins utilizes a different mechanism that is likely specific to each organelle's limiting membrane.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.