FAK auto-phosphorylation site tyrosine 397 is required for development but dispensable for normal skin homeostasis.
Focal adhesion kinase (FAK) is an intensely studied non-receptor tyrosine kinase with roles in cancer and other common human diseases. Despite the large interest in FAK, the in vivo contribution of FAK auto-phosphorylation site tyrosine (Y) 397 to FAK function is incompletely understood. To study FA...
Main Authors: | Joel B Heim, Cera A McDonald, Saranya P Wyles, Sindhuja Sominidi-Damodaran, Edwin J Squirewell, Ming Li, Catherine Motsonelidze, Ralph T Böttcher, Jan van Deursen, Alexander Meves |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2018-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC6042779?pdf=render |
Similar Items
-
High resolution crystal structure of the FAK FERM domain reveals new insights on the Druggability of tyrosine 397 and the Src SH3 binding site
by: Timothy Marlowe, et al.
Published: (2019-05-01) -
Tyrosine phosphorylation of cortactin by the FAK-Src complex at focal adhesions regulates cell motility
by: Wang Wenqi, et al.
Published: (2011-11-01) -
pFAK-Y397 overexpression as both a prognostic and a predictive biomarker for patients with metastatic osteosarcoma.
by: Kamolrat Thanapprapasr, et al.
Published: (2017-01-01) -
Correction: pFAK-Y397 overexpression as both a prognostic and a predictive biomarker for patients with metastatic osteosarcoma.
by: PLOS ONE Staff
Published: (2017-01-01) -
Redox Regulation of NOX Isoforms on FAK<sup>(Y397)</sup>/SRC<sup>(Y416)</sup> Phosphorylation Driven Epithelial-to-Mesenchymal Transition in Malignant Cervical Epithelial Cells
by: Young Mee Kim, et al.
Published: (2020-06-01)