TRIB1
Tribbles homolog 1 is a
Function
Tribbles-1 is one of three members of the Tribbles subfamily, which is a part of the CAMK Ser/Thr protein kinase family, of the protein kinase superfamily. The Tribbles subfamily is one of the pseudokinases, meaning that while expressing putative kinase regions in its structure, it is non-catalytic. The Tribbles subfamily lacks a functional ATP binding pocket, and therefore cannot phosphorylate its substrates; instead, Tribbles proteins function as scaffold proteins, which bind their substrates to localize them to or from their function [8]
Expression of Tribbles-1 is highly variable, constantly changing with respect to time and cell-type,[11] which suggests a large amount of regulation that exists in the cell. The protein's primary structure contains a PEST region, indicative of proteins that are highly susceptible to degradation in the cell; Tribbles-1 plays a role in regulating its own expression by binding to its substrate, which not only produces its function on the MAPK pathway, but also works to protect it from degradation whilst binding. This, in part, creates a positive feedback loop in the function of Tribbles-1, as the function of Tribbles-1 directly aids in the increase of the amount of it. As positive feedback loops are often seen throughout biology in circumstances that require the alleviation of an external stimulus, the positive feedback loop exhibited by Tribbles-1 suggests that it plays a functional role in cell response.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000173334 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032501 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 9342215.
- S2CID 24556931.
- ^ "Entrez Gene: TRIB1 tribbles homolog 1 (Drosophila)".
- ^ PMID 27908682.
- PMID 26455797.
- PMID 26517930.
- PMID 16364454.
Further reading
- Tang K, Finley RL, Nie D, Honn KV (March 2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry. 39 (12): 3185–91. PMID 10727209.
- Wu M, Xu LG, Zhai Z, Shu HB (July 2003). "SINK is a p65-interacting negative regulator of NF-kappaB-dependent transcription". The Journal of Biological Chemistry. 278 (29): 27072–9. PMID 12736262.
- Kiss-Toth E, Bagstaff SM, Sung HY, Jozsa V, Dempsey C, Caunt JC, et al. (October 2004). "Human tribbles, a protein family controlling mitogen-activated protein kinase cascades". The Journal of Biological Chemistry. 279 (41): 42703–8. PMID 15299019.
- Xu C, Zhang J, Huang X, Sun J, Xu Y, Tang Y, et al. (June 2006). "Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP". The Journal of Biological Chemistry. 281 (23): 15900–8. PMID 16595688.
- Sung HY, Guan H, Czibula A, King AR, Eder K, Heath E, et al. (June 2007). "Human tribbles-1 controls proliferation and chemotaxis of smooth muscle cells via MAPK signaling pathways". The Journal of Biological Chemistry. 282 (25): 18379–87. PMID 17452330.
External links
- TRIB1 human gene location in the UCSC Genome Browser.
- TRIB1 human gene details in the UCSC Genome Browser.
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