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Related Concept Videos

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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Regulation of Nuclear Protein Sorting01:45

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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 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.
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Non-LTR Retrotransposons03:18

Non-LTR Retrotransposons

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As the name suggests, non-LTR retrotransposons lack the long terminal repeats characteristic of the LTR retrotransposons. Additionally, both LTR and non-LTR retrotransposons use distinct mechanisms of mobilization. Non-LTR retrotransposons are further divided into two classes - Long interspersed nuclear elements (LINEs) and short interspersed nuclear elements (SINEs), both of which occur abundantly in most mammals, including humans. Some of the active non-LTR retrotransposons in humans are L1...
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Analysis of Spliceosomal snRNA Localization in Human Hela Cells Using Microinjection
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Multiple nuclear localization sequences in SRSF4 protein.

So Masaki1,2, Takafumi Kabuto3, Kenji Suzuki2

  • 1Laboratory for Malignancy Control Research, Medical Innovation Center, Kyoto University Graduate School of Medicine, Kyoto, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|February 13, 2020
PubMed
Summary
This summary is machine-generated.

The serine-/arginine (SR)-rich splicing factor 4 (SRSF4) protein

Keywords:
NLSRS domainSR repeatSRSF4classical-type NLS

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • The serine-/arginine (SR)-rich protein family plays a crucial role in RNA splicing.
  • SRSF4, a member of this family, is known to be localized in the nucleus.
  • The specific nuclear localization signals (NLSs) for SRSF4 have not been previously identified.

Purpose of the Study:

  • To identify and characterize the nuclear localization signals (NLSs) of SRSF4.
  • To investigate the functional domains responsible for SRSF4 nuclear import.
  • To elucidate the mechanisms governing SRSF4's localization within the nucleus.

Main Methods:

  • Utilized a pyruvate kinase (PK) fusion system to assay for nuclear localization.
  • Fused SRSF4 domains to PK protein to determine their NLS activity.
  • Delineated minimum sequences within the RS domain responsible for nuclear import.

Main Results:

  • The arginine-/serine (RS)-rich domain of SRSF4 confers nuclear localization activity when fused to PK.
  • Identified specific minimum sequences within the RS domain essential for nuclear import.
  • Discovered that the RS-rich region does not consistently confer nuclear localization, and identified classical-type NLS-like sequences.

Conclusions:

  • SRSF4 possesses multiple NLSs within its RS domain.
  • SRSF4 likely utilizes at least two distinct nuclear import pathways.
  • These findings provide new insights into the regulation of SRSF4 localization and function.