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
Summary
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.
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.
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