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Related Concept Videos

Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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Nuclear Protein Sorting01:34

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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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Nuclear Export of mRNA02:31

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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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Nuclear Localization Signals and Import01:46

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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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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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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells
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Phosphate-dependent nuclear export via a novel NES class recognized by exportin Msn5.

Ho Yee Joyce Fung, Sanraj R Mittal, Ashley B Niesman

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    Yeast exportin Msn5 recognizes a novel phosphorylated nuclear export signal (NES) on transcription factor Pho4. This phosphate-specific interaction and Msn5 autoinhibition reveal new mechanisms for nuclear transport regulation.

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    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Structural Biology

    Background:

    • Nuclear transport of signaling proteins is crucial for gene expression regulation.
    • Phosphorylation of signaling proteins often dictates their subcellular localization and function.
    • The yeast exportin Msn5 mediates nuclear export, but its cargo recognition mechanisms are not fully understood.

    Purpose of the Study:

    • To elucidate the structural basis of the interaction between the yeast exportin Msn5 and its cargo, the phosphate-sensing transcription factor Pho4.
    • To uncover the mechanism by which Pho4 phosphorylation regulates its nuclear export.
    • To investigate the autoinhibitory mechanism of Msn5 and its implications for cargo binding.

    Main Methods:

    • Cryogenic-electron microscopy (cryo-EM) to determine the structure of Msn5 bound to Pho4.
    • Biochemical assays to study protein-protein interactions and binding kinetics.
    • Site-directed mutagenesis to probe the role of specific residues in binding and export.

    Main Results:

    • Pho4 utilizes a novel, extended phosphorylated 35-residue nuclear export signal (NES) that binds to the concave surface of Msn5.
    • Two phosphorylated serine residues in Pho4 directly interact with basic patches on Msn5, mediating phosphate-specific recognition.
    • Unliganded Msn5 is autoinhibited, and Pho4 binding, along with Ran binding, overcomes this inhibition, facilitating Pho4 release in the cytoplasm.

    Conclusions:

    • The study reveals a previously unknown mechanism of phosphate-specific recognition in nuclear transport, mediated by a novel NES.
    • Msn5's autoinhibitory mechanism explains the cooperativity of cargo binding and release, providing insights into regulated nuclear export.
    • These findings expand the understanding of diverse nuclear export signals and the critical role of cargo phosphorylation in cellular signaling.