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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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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 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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Mitochondrial Protein Sorting01:39

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
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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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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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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Related Experiment Video

Updated: Aug 9, 2025

Isolation of CA1 Nuclear Enriched Fractions from Hippocampal Slices to Study Activity-dependent Nuclear Import of Synapto-nuclear Messenger Proteins
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Mitochondrial-nuclear communication by FKBP51 shuttling.

Nadia Zgajnar1, Mariana Lagadari2, Luciana I Gallo3

  • 1Instituto de Biología y Medicina Experimental (IBYME)/CONICET, Buenos Aires, Argentina.

Journal of Cellular Biochemistry
|February 23, 2023
PubMed
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FKBP51 protein shuttles between mitochondria and the nucleus, regulating cell stress responses and telomerase activity. This mitochondrial-nuclear trafficking impacts cell differentiation, apoptosis, and recovery from stress.

Keywords:
apoptosiscancerimmunophilinmitochondriashuttlingstress

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • FKBP51 is an HSP90-binding immunophilin with structural similarity to FKBP52, but distinct functions.
  • Immunophilins FKBP51 and FKBP52 were initially identified in steroid receptor complexes, crucial for steroid receptor activation.
  • Emerging roles for FKBP51 include cell differentiation, apoptosis, metabolic, and psychiatric disorders.

Purpose of the Study:

  • To review recent findings on FKBP51's role in mitochondrial-nuclear communication.
  • To explore the implications of FKBP51's dynamic localization in cellular homeostasis and stress response.

Main Methods:

  • Literature review of studies investigating FKBP51 localization and function.
  • Analysis of FKBP51's interaction with mitochondria, nucleus, and its impact on cellular processes.

Main Results:

  • FKBP51 is found in mitochondria, exerting antiapoptotic effects via its tetratricopeptide repeats domains.
  • Upon cell differentiation or stress, FKBP51 translocates to the nucleus, enhancing telomerase activity.
  • This mitochondrial-nuclear trafficking is reversible, influenced by factors like viral infections.

Conclusions:

  • FKBP51 acts as a key mediator of communication between mitochondria and the nucleus.
  • FKBP51's dynamic localization is critical for managing cellular stress, differentiation, and potentially aging.
  • Further research into FKBP51-mediated signaling could reveal novel therapeutic targets.