Abstract
This chapter focuses on published studies specifically concerning TCTP and its involvement in degradation or stabilization of various proteins, and also in its own degradation in different ways. The first part relates to the inhibition of proteasomal degradation of proteins. This can be achieved by masking ubiquitination sites of specific partners, by favoring ubiquitin E3 ligase degradation, or by regulating proteasome activity. The second part addresses the ability of TCTP to favor degradation of specific proteins through proteasome or macroautophagic pathways. The third part discusses about the different ways by which TCTP has been shown to be degraded.
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- Bre5:
-
Brefeldin A sensitivity 5
- CMA:
-
Chaperone-mediated autophagy
- DHA:
-
Dihydroartemisinin
- HIF1α:
-
Hypoxia-inducible factor 1α
- HRF:
-
Histamine releasing factor
- Hsp27:
-
Heat shock protein 27
- Mcl-1:
-
Myeloid cell leukemia 1
- Mdm2:
-
Murine double minute 2
- Mmi1:
-
Microtubule and mitochondria interacting protein
- Mss4:
-
Mammalian suppressor of yeast Sec4
- Mst-1:
-
Mammalian sterile twenty-1
- NTHK1:
-
Tobacco histidine kinase-1
- Pim-3:
-
Serine/threonine-protein kinase Pim-3
- PRX1:
-
Peroxiredoxin-1
- Rpn:
-
26S proteasome regulatory subunit
- Rpt:
-
Proteasome regulatory particle base subunit
- UPS:
-
Ubiquitin–proteasome system
- TCTP:
-
Translationally controlled tumor protein
- Ubp3:
-
ubiquitin specific protease 3
- VHL:
-
von Hippel–Lindau protein
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Acknowledgements
This work was supported by grants from the CNRS, the University of Montpellier, and from the Labex LERMIT.
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Vidal, M. (2017). Role and Fate of TCTP in Protein Degradative Pathways. In: Telerman, A., Amson, R. (eds) TCTP/tpt1 - Remodeling Signaling from Stem Cell to Disease. Results and Problems in Cell Differentiation, vol 64. Springer, Cham. https://doi.org/10.1007/978-3-319-67591-6_6
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