Literature summary for 6.1.1.1 extracted from

Vo, M.N.; Yang, X.L.; Schimmel, P.
Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase (2011), J. Biol. Chem., 286, 11563-11568.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Synonyms

Synonyms	Comment	Organism
Tyrosyl-tRNA synthetase	-	Homo sapiens
TyrRS	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	dissociating quaternary structures regulating novel functions of other tRNA synthetases	Homo sapiens
physiological function	although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRSMini, which not only has the same aminoacylation activity as native TyrRS when occuring as a dimer, the monomer is inactive, but TyrRSMini also has strong activity for stimulating migration of polymorphonuclear leukocytes. The migration-stimulating activity is dependent on an ELR tripeptide motif, similar to that in CXC cytokines like IL-8, and also has the familiar bell-shaped concentration dependence seen for CXC cytokines. But TyrRSMini does not induce internalization of CXCR1/2. The TyrRSMini monomer is an agonist, while TyrRSMini dimer is an antagonist of induced PMN cell migration	Homo sapiens

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Release 2023.1 (January 2023)