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Biochem Biophys Res Commun. 2017 Aug 26;490(3):1074-1079. doi: 10.1016/j.bbrc.2017.06.168. Epub 2017 Jun 28.

Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites.

Author information

1
Department of Pathology, University of Pittsburgh, Pittsburgh, PA 15213, United States.
2
Department of Biological Engineering, MIT, Cambridge, MA 02319, United States.
3
Department of Pathology, University of Pittsburgh, Pittsburgh, PA 15213, United States; Pittsburgh VA Health System, Pittsburgh, PA 15213, United States. Electronic address: wellsa@upmc.edu.

Abstract

Tyro3, a member of TAM receptor tyrosine kinase family has been suggested to be autophosphorylated upon activation. In the current study we mapped the autophosphorylation sites of murine Tyro3 to tyrosine 723 and 756, with K540 being required for its kinase activity. Knockdown of Axl significantly decreases the tyrosyl-phosphorylation of Tyro3 in fibroblasts NR6WT, suggesting an interaction among the TAM family members. Interestingly, the carboxyl terminal region of Tyro3 is required for its stability in cells with a minimal length of 1-778 amino acids which is not conserved in murine Axl, a member of TAM. These data suggest that the autophosphorylation sites of TAM RTK members are unique although they share high similarity in amino acids within their carboxyl kinase domain.

KEYWORDS:

Autophosphorylation; Protein stability; TAM family kinases; Tyro3 receptor tyrosine kinase

PMID:
28668391
PMCID:
PMC5553559
DOI:
10.1016/j.bbrc.2017.06.168
[Indexed for MEDLINE]
Free PMC Article

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