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Related Concept Videos

Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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Microtubules in Signaling01:22

Microtubules in Signaling

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The primary cilium, made up of microtubules, acts as antennae on the cell surfaces for relaying external stimuli into the cells. These fine hair-like structures are present, generally one per cell. These are non-motile cilia in a 9+0 microtubules arrangement, where the central pair of microtubules are absent. The primary cilia arise from the basal body embedded in the cell membrane. Intraflagellar transport (IFT) carries requisite proteins from the cytoplasm to the cilium because the primary...
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Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

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Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Related Experiment Video

Updated: Mar 1, 2026

Artificial Intelligence Approaches to Assessing Primary Cilia
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Nuclear roles for cilia-associated proteins.

Tristan D McClure-Begley1, Michael W Klymkowsky1

  • 1Molecular, Cellular and Developmental Biology, University of Colorado Boulder, Boulder, CO 80309 USA.

Cilia
|June 1, 2017
PubMed
Summary

Cilia and nuclear pores share transport machinery, explaining why ciliary proteins function in the nucleus. Understanding these nuclear roles is crucial for interpreting ciliogenesis defects.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Cilia are evolutionarily ancient structures involved in cellular functions.
  • The ciliary gate controls molecular traffic between cellular compartments.
  • Nuclear pores regulate transport between the cytoplasm and the nucleus.

Purpose of the Study:

  • To investigate the hypothesis that shared transport machinery exists between cilia and the nucleus.
  • To explore the nuclear functions of ciliary and ciliogenesis-associated proteins.
  • To understand the implications of nuclear roles for ciliary disease phenotypes.

Main Methods:

  • Comparative analysis of ciliary gate and nuclear pore structures.
  • Bioinformatic analysis of ciliary protein localization and function.

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  • Literature review on nuclear roles of ciliary proteins.

    • Main Results:

    • The ciliary gate shares structural and functional similarities with nuclear pores.
    • Numerous ciliary proteins are found in the nucleus, regulating gene expression, DNA repair, and transport.
    • These nuclear functions contribute to the phenotypic outcomes of mutations in ciliary genes.

    Conclusions:

    • Shared molecular machinery underlies the nuclear localization and function of ciliary proteins.
    • Nuclear roles of ciliary proteins are critical for understanding ciliopathies.
    • Further research into these dual roles will advance knowledge of cilia and nuclear transport.