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NEDD8, ISG15 and FAT10
See also
Selected Literature
Ubiquitin & Ubl Signaling Catalog
FAT10
FAT10 is a small ubiquitin-like modifier that is encoded in the major histocompatibility complex and is synergistically inducible by tumor necrosis factor alpha and gamma-interferon. It is composed of two ubiquitin-like domains and possesses a free C-terminal diglycine motif that is required for the formation of FAT10 conjugates. FAT10 conjugates are rapidly degraded by the proteasome. Conjugation with FAT10 may thus provide an alternative ubiquitin-independent targeting mechanism for degradation by the proteasome, which is both cytokine inducible and irreversible. FAT10 has been shown to interact with the histone deacetylase HDAC6 which, in the absence of proteasomal degradation, may provide an alternative route to protein sequestration and removal by transporting conjugates to the aggresome. Again, as with ISG15 modification, a role in malignant transformation has been proposed.
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Literature References
- FAT10, a ubiquitin-independent signal for proteasomal degradation: M.S. Hipp, et al.; Mol. Cell Biol. 25, 3483 (2005).
- The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition: B. Kalveram, et al.; J. Cell Sci. 121, 4079 (2008)
- FAT10 level in human gastric cancer and its relation with mutant p53 level, lymph node metastasis and TNM staging: F. Ji, et al.; World J. Gastroenterol. 15, 2228 (2009)
NEDD8
NEDD8 is a small ubiquitin-like protein that can be conjugated to substrate-proteins in a process known as NEDDylation.
Although NEDDylation plays a critical regulatory role in cell growth, viability, and development, the spectrum of NEDD8 substrates and its interaction network remains the subject of much investigation. Originally believed to modify only the cullin family members, it is now recognized that a large number of NEDD8 modified and associated proteins are involved in transcription, DNA repair and replication, cell cycle regulation and chromatin organization, and remodeling.
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Literature References
- A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins: J. Jones, et al.; J. Proteome Res. 7, 1274 (2008)
- Novel substrates and functions for the ubiquitin-like molecule NEDD8: D.P. Xirodimas; Biochem. Soc. Trans. 36, 802 (2008)
- The mechanism of poly-NEDD8 chain formation in vitro: Y. Ohki, et al.; BBRC 381, 443 (2009)
ISG15
A lesser appreciated and understood member of the ubiquitin-like protein family is ISG15, a modifier encoded by an interferon stimulated gene. ISG15 has been ascribed important functions in various biological pathways from pregnancy to innate immune responses. Furthermore, ISG15 has been found to modify several important molecules and affect type I interferon signal transduction. Much further work is required in order to further elucidate the biological consequences of ISG15 and ISG15 modification, although its role in certain disease states such as malignant transformation has recently been proposed.
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Literature References
- ISG15: the immunological kin of ubiquitin: K.J. Ritchie & D.E. Zhang; Semin. Cell Dev. Biol. 15, 237 (2004)
- Expression, regulation and function of the ISGylation system in prostate cancer: A. Kiessling, et al.; Oncogene 28, 2606 (2009)
