Difference between revisions of "Kinase Family Trbl"
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Trbl ("tribbles") is a family of pseudokinases involved in protein interactions and ubiquitination. | Trbl ("tribbles") is a family of pseudokinases involved in protein interactions and ubiquitination. | ||
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====Evolution==== | ====Evolution==== | ||
Trbl is found throughout animals. Nematodes have a highly divergent member, originally classified as Other-Unique. Vertebrates have 3, TRBL1, TRBL2, TRBL3. | Trbl is found throughout animals. Nematodes have a highly divergent member, originally classified as Other-Unique. Vertebrates have 3, TRBL1, TRBL2, TRBL3. | ||
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====Domain Structure==== | ====Domain Structure==== | ||
| − | Trbl has a divergent kinase domain, followed by a COP1 degron, and a unique C-terminal tail. | + | Trbl has a divergent kinase domain, followed by a MEK1-binding motif (ILDHPWF in human TRIB2), a COP1 degron (DQLVP in human TRIB2), and a unique C-terminal tail. The COP1 domain is degraded in nematodes and some insects that have lost COP1, including Drosophila, and the MEK1 motif also appears degraded in those same insects. |
| + | ====Functions==== | ||
| + | Trbl has a variety of functions, mostly as a modulated scaffold that brings other proteins together. | ||
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| + | In Drosophila, trbl binds binds and degrades a number of proteins, including the cdc25 phosphatase string, to control cell cycle, and the C/EBP protein slbo, to control cell migration | ||
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Modulation of CEBP function is conserved in C. elegans, helping to define the highly divergent gene nipi-3 (K09A9.1) as a member of the Trbl family <cite>Kim, McEwan</cite>. | Modulation of CEBP function is conserved in C. elegans, helping to define the highly divergent gene nipi-3 (K09A9.1) as a member of the Trbl family <cite>Kim, McEwan</cite>. | ||
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====References==== | ====References==== | ||
Revision as of 02:34, 17 February 2017
Kinase Classification: Group CAMK: Family Trbl
Trbl ("tribbles") is a family of pseudokinases involved in protein interactions and ubiquitination.
Evolution
Trbl is found throughout animals. Nematodes have a highly divergent member, originally classified as Other-Unique. Vertebrates have 3, TRBL1, TRBL2, TRBL3.
Domain Structure
Trbl has a divergent kinase domain, followed by a MEK1-binding motif (ILDHPWF in human TRIB2), a COP1 degron (DQLVP in human TRIB2), and a unique C-terminal tail. The COP1 domain is degraded in nematodes and some insects that have lost COP1, including Drosophila, and the MEK1 motif also appears degraded in those same insects.
Functions
Trbl has a variety of functions, mostly as a modulated scaffold that brings other proteins together.
In Drosophila, trbl binds binds and degrades a number of proteins, including the cdc25 phosphatase string, to control cell cycle, and the C/EBP protein slbo, to control cell migration
Modulation of CEBP function is conserved in C. elegans, helping to define the highly divergent gene nipi-3 (K09A9.1) as a member of the Trbl family [1, 2].
References
- Kim KW, Thakur N, Piggott CA, Omi S, Polanowska J, Jin Y, and Pujol N. Coordinated inhibition of C/EBP by Tribbles in multiple tissues is essential for Caenorhabditis elegans development. BMC Biol. 2016 Dec 7;14(1):104. DOI:10.1186/s12915-016-0320-z |
- McEwan DL, Feinbaum RL, Stroustrup N, Haas W, Conery AL, Anselmo A, Sadreyev R, and Ausubel FM. Tribbles ortholog NIPI-3 and bZIP transcription factor CEBP-1 regulate a Caenorhabditis elegans intestinal immune surveillance pathway. BMC Biol. 2016 Dec 7;14(1):105. DOI:10.1186/s12915-016-0334-6 |
