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Related Concept Videos

Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Nuclear Export01:42

Nuclear Export

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

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Related Experiment Video

Updated: Jun 14, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

RanGTPase: A Key Regulator of Nucleocytoplasmic Trafficking.

Ki Lui1, Ying Huang

  • 1Department of Pharmacology, State University of New York, Upstate Medical University, Syracuse, New York.

Molecular and Cellular Pharmacology
|September 28, 2011
PubMed
Summary
This summary is machine-generated.

RanGTPase, a key regulator of nucleocytoplasmic transport and cell division, is essential for cell viability. Its dysregulation is linked to cancer development, highlighting its critical role in cellular processes.

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Last Updated: Jun 14, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • RanGTPase, a member of the Ras superfamily, is predominantly nuclear and regulates vital cellular functions.
  • It controls nucleocytoplasmic trafficking, mitotic spindle assembly, and nuclear envelope formation.
  • RanGTPase's function relies on its GTP/GDP-bound states and interaction with karyopherins, NTF2, and nucleoporins.

Purpose of the Study:

  • To elucidate the multifaceted roles of RanGTPase in cellular regulation.
  • To understand the mechanism of RanGTPase in nucleocytoplasmic transport.
  • To explore the implications of RanGTPase dysregulation in tumorigenesis.

Main Methods:

  • Literature review and synthesis of existing research on RanGTPase.
  • Analysis of RanGTPase's interactions with key cellular components.
  • Examination of the functional consequences of altered RanGTPase expression.

Main Results:

  • RanGTPase governs directional nucleocytoplasmic transport via distinct import and export mechanisms.
  • GTP-bound Ran dissociates importin:cargo complexes in the nucleus and facilitates exportin:cargo complex transport.
  • RanGTPase is crucial for cell viability, and its overexpression correlates with tumorigenesis.

Conclusions:

  • RanGTPase is indispensable for fundamental cellular events, including transport and cell division.
  • Aberrant RanGTPase activity and expression are implicated in cancer pathogenesis.
  • Targeting RanGTPase pathways may offer therapeutic strategies for cancer treatment.