Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites
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 d...
| Main Authors: | , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Published: |
Elsevier
2018
|
| Online Access: | http://hdl.handle.net/1721.1/117689 https://orcid.org/0000-0002-0050-989X |
| _version_ | 1826197572229791744 |
|---|---|
| author | Shao, Hanshuang Wells, Alan Lauffenburger, Douglas A |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Shao, Hanshuang Wells, Alan Lauffenburger, Douglas A |
| author_sort | Shao, Hanshuang |
| collection | MIT |
| description | 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: Tyro3 receptor tyrosine kinase; Autophosphorylation; Protein stability; TAM family kinases |
| first_indexed | 2024-09-23T10:49:44Z |
| format | Article |
| id | mit-1721.1/117689 |
| institution | Massachusetts Institute of Technology |
| last_indexed | 2024-09-23T10:49:44Z |
| publishDate | 2018 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/1176892022-09-30T23:20:17Z Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites Shao, Hanshuang Wells, Alan Lauffenburger, Douglas A Massachusetts Institute of Technology. Department of Biological Engineering Lauffenburger, Douglas A 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: Tyro3 receptor tyrosine kinase; Autophosphorylation; Protein stability; TAM family kinases National Institute of General Medical Sciences (U.S.) (Award GM69668) National Institute of General Medical Sciences (U.S.) (Award GM63569) 2018-09-10T18:49:24Z 2018-09-10T18:49:24Z 2017-06 2017-06 2018-09-07T19:22:43Z Article http://purl.org/eprint/type/JournalArticle 0006-291X 1090-2104 http://hdl.handle.net/1721.1/117689 Shao, Hanshuang et al. “Tyro3 Carboxyl Terminal Region Confers Stability and Contains the Autophosphorylation Sites.” Biochemical and Biophysical Research Communications 490, 3 (August 2017): 1074–1079 © 2017 Elsevier Inc https://orcid.org/0000-0002-0050-989X http://dx.doi.org/10.1016/J.BBRC.2017.06.168 Biochemical and Biophysical Research Communications Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier PMC |
| spellingShingle | Shao, Hanshuang Wells, Alan Lauffenburger, Douglas A Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title | Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title_full | Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title_fullStr | Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title_full_unstemmed | Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title_short | Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| title_sort | tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites |
| url | http://hdl.handle.net/1721.1/117689 https://orcid.org/0000-0002-0050-989X |
| work_keys_str_mv | AT shaohanshuang tyro3carboxylterminalregionconfersstabilityandcontainstheautophosphorylationsites AT wellsalan tyro3carboxylterminalregionconfersstabilityandcontainstheautophosphorylationsites AT lauffenburgerdouglasa tyro3carboxylterminalregionconfersstabilityandcontainstheautophosphorylationsites |