نتایج جستجو برای: fak

تعداد نتایج: 3501  

Journal: :Circulation research 2008
Talita M Marin Carolina F M Z Clemente Aline M Santos Paty K Picardi Vinícius D B Pascoal Iscia Lopes-Cendes Mário J A Saad Kleber G Franchini

The aim of this study was to investigate whether Shp2 (Src homology region 2, phosphatase 2) controls focal adhesion kinase (FAK) activity and its trophic actions in cardiomyocytes. We show that low phosphorylation levels of FAK in nonstretched neonatal rat ventricular myocytes (NRVMs) coincided with a relatively high basal association of FAK with Shp2 and Shp2 phosphatase activity. Cyclic stre...

2017
Kazuo Katoh

Specific regulation and activation of focal adhesion kinase (FAK) are thought to be important for focal adhesion formation, and activation of Rho-kinase has been suggested to play a role in determining the effects of FAK on the formation of stress fibers and focal adhesions. To clarify the role of FAK in stress fiber formation and focal adhesion organization, the author examined the formation o...

Journal: :International journal of oncology 2016
Iliet Payan Susan McDonnell Haydee M Torres Wim F A Steelant Séverine Van Slambrouck

Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase known to promote cell migration and invasiveness. Overexpression and increased activity of FAK are closely associated with metastatic breast tumors and are linked to poor prognosis. This study discovered an inverse correlation between FAK activity and migratory and invasive behavior. We show decreased phosphorylation levels of FAK at...

2014
Xuqian Fang Xiangfan Liu Ling Yao Changqiang Chen Jiafei Lin Peihua Ni Xinmin Zheng Qishi Fan

Mounting evidence suggests that the FAK N-terminal (FERM) domain controls FAK phosphorylation and function; however, little is known regarding the role of the C terminal (FAT) domain in FAK regulation. We identified a patient-derived FAK mutant, in which a 27-amino acid segment was deleted from the C-terminal FAT domain (named FAK-Del33). When FAK-Del33 was overexpressed in specific tumor cell ...

Journal: :Molecular biology of the cell 1999
M D Schaller J D Hildebrand J T Parsons

Tyrosine phosphorylation of focal adhesion kinase (FAK) creates a high-affinity binding site for the src homology 2 domain of the Src family of tyrosine kinases. Assembly of a complex between FAK and Src kinases may serve to regulate the subcellular localization and the enzymatic activity of members of the Src family of kinases. We show that simultaneous overexpression of FAK and pp60(c-src) or...

Journal: :Clinical cancer research : an official journal of the American Association for Cancer Research 2000
W G Cance J E Harris M V Iacocca E Roche X Yang J Chang S Simkins L Xu

The focal adhesion kinase (FAK) is a protein tyrosine kinase linked to signaling events between cells and the extracellular matrix. Studies at the Western blot level have demonstrated up-regulation of FAK expression in invasive breast and colon cancers. To assess p125FAK expression at the cellular level, we developed monoclonal antibodies that specifically detected FAK in formalin-fixed, paraff...

Journal: :Neoplasia 2003
Bhumsoo Kim Cynthia M van Golen Eva L Feldman

Focal adhesion kinase (FAK) prevents apoptosis in many cell types. We have reported that tyrosine residues in FAK are dephosphorylated and FAK is degraded during mannitol-induced apoptosis in human neuroblastoma cells. Several studies suggest that FAK dephosphorylation and degradation are separate events. The current study defines the relationship between FAK dephosphorylation and degradation i...

Journal: :Journal of cell science 2012
Oisun Jung Suyong Choi Sun-Bok Jang Sin-Ae Lee Ssang-Taek Lim Yoon-Ju Choi Hye-Jin Kim Do-Hee Kim Tae Kyoung Kwak Hyeonjung Kim Minkyung Kang Mi-Sook Lee Sook Young Park Jihye Ryu Doyoung Jeong Hae-Kap Cheong Hyun Jeong Kim Ki Hun Park Bong-Jin Lee David D Schlaepfer Jung Weon Lee

Transmembrane 4 L six family member 5 (TM4SF5) plays an important role in cell migration, and focal adhesion kinase (FAK) activity is essential for homeostatic and pathological migration of adherent cells. However, it is unclear how TM4SF5 signaling mediates the activation of cellular migration machinery, and how FAK is activated during cell adhesion. Here, we showed that direct and adhesion-de...

Journal: :Cellular & molecular biology letters 2001
Joanna Miloszewska Halina Trembacz Maciej Malecki Przemyslaw Janik

Non-transformed cells cultivated in vitro become contact inhibited (stop growing) when they reach confluence at the level which is called a saturation density. Our previous study documented that in contact inhibited C3H10T1/2 fibroblasts MAP kinase (MAPK) has not been activated by serum or fibronectin, whereas in fast growing (sparse) MAPK was evidently stimulated. The same schedule of the reac...

Journal: :The Journal of Cell Biology 2005
Naciba Benlimame Qiang He Su Jie Dingzhang Xiao Ying Jie Xu Martin Loignon David D. Schlaepfer Moulay A. Alaoui-Jamali

The overexpression of members of the ErbB tyrosine kinase receptor family has been associated with cancer progression. We demonstrate that focal adhesion kinase (FAK) is essential for oncogenic transformation and cell invasion that is induced by ErbB-2 and -3 receptor signaling. ErbB-2/3 overexpression in FAK-deficient cells fails to promote cell transformation and rescue chemotaxis deficiency....

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