Results 21 to 30 of about 51,195 (186)

Receptor Protein-tyrosine Phosphatase α Regulates Focal Adhesion Kinase Phosphorylation and ErbB2 Oncoprotein-mediated Mammary Epithelial Cell Motility [PDF]

Journal of Biological Chemistry, 2013
We investigated the role of protein-tyrosine phosphatase α (PTPα) in regulating signaling by the ErbB2 oncoprotein in mammary epithelial cells. Using this model, we demonstrated that activation of ErbB2 led to the transient inactivation of PTPα, suggesting that attenuation of PTPα activity may contribute to enhanced ErbB2 signaling.
Boivin, Benoit, Chaudhary, Fauzia, Dickinson, Bryan C, Haque, Aftabul, Pero, Stephanie C, Chang, Christopher J, Tonks, Nicholas K   +6 more
openaire   +4 more sources

Prolactin-induced protein (PIP) regulates proliferation of luminal A type breast cancer cells in an estrogen-independent manner. [PDF]

PLoS ONE, 2014
Prolactin-induced Protein (PIP), an aspartyl protease unessential for normal mammalian cell function, is required for the proliferation and invasion of some breast cancer (BCa) cell types.
Sanjeev K Baniwal, Nyam-Osor Chimge, V Craig Jordan, Debu Tripathy, Baruch Frenkel   +4 more
doaj   +1 more source

Non-overlapping functions for Pyk2 and FAK in osteoblasts during fluid shear stress-induced mechanotransduction. [PDF]

PLoS ONE, 2011
Mechanotransduction, the process by which cells convert external mechanical stimuli such as fluid shear stress (FSS) into biochemical changes, plays a critical role in maintenance of the skeleton.
Suzanne R L Young, Julia M Hum, Eric Rodenberg, Charles H Turner, Fredrick M Pavalko   +4 more
doaj   +1 more source

SH2 Domain-Containing Protein Tyrosine Phosphatase 2 and Focal Adhesion Kinase Protein Interactions Regulate Pulmonary Endothelium Barrier Function [PDF]

American Journal of Respiratory Cell and Molecular Biology, 2015
Enhanced protein tyrosine phosphorylation is associated with changes in vascular permeability through formation and dissolution of adherens junctions and regulation of stress fiber formation. Inhibition of the protein tyrosine phosphorylase SH2 domain-containing protein tyrosine phosphatase 2 (SHP2) increases tyrosine phosphorylation of vascular ...
Havovi, Chichger, Julie, Braza, Huetran, Duong, Elizabeth O, Harrington   +3 more
openaire   +2 more sources

Recruitment of focal adhesion kinase and paxillin to β1 integrin promotes cancer cell migration via mitogen activated protein kinase activation

BMC Cancer, 2004
Background Integrin-extracellular matrix interactions activate signaling cascades such as mitogen activated protein kinases (MAPK). Integrin binding to extracellular matrix increases tyrosine phosphorylation of focal adhesion kinase (FAK).
Ohannessian Arthur, Crowe David L
doaj   +1 more source

Oxidative stress‐induced FAK activation contributes to uterine serous carcinoma aggressiveness

Molecular Oncology, 2023
Uterine serous carcinoma (USC) is an aggressive form of endometrial cancer (EC), characterized by its high propensity for metastases. In fact, while endometrioid endometrial carcinoma (EEC), which accounts for 85% of EC, presents a good prognosis, USC is
Isabel C. Lopez‐Mejia, Jordi Pijuan, Raúl Navaridas, Maria Santacana, Sònia Gatius, Ana Velasco, Gerard Castellà, Anaïs Panosa, Elisa Cabiscol, Miquel Pinyol, Laura Coll, Núria Bonifaci, Laura Plata Peña, August Vidal, Alberto Villanueva, Eloi Gari, David Llobet‐Navàs, Lluis Fajas, Xavier Matias‐Guiu, Andrée Yeramian   +19 more
doaj   +1 more source

The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases

Frontiers in Synaptic Neuroscience, 2021
Pyk2 is a non-receptor tyrosine kinase highly enriched in forebrain neurons. Pyk2 is closely related to focal adhesion kinase (FAK), which plays an important role in sensing cell contacts with extracellular matrix and other extracellular signals ...
Benoit de Pins, Benoit de Pins, Benoit de Pins, Tiago Mendes, Tiago Mendes, Tiago Mendes, Albert Giralt, Albert Giralt, Albert Giralt, Albert Giralt, Jean-Antoine Girault, Jean-Antoine Girault, Jean-Antoine Girault   +12 more
doaj   +1 more source

LNK (SH2B3): paradoxical effects in ovarian cancer. [PDF]

, 2015
LNK (SH2B3) is an adaptor protein studied extensively in normal and malignant hematopoietic cells. In these cells, it downregulates activated tyrosine kinases at the cell surface resulting in an antiproliferative effect. To date, no studies have examined
Chien, W, Ding, L-W, Doan, NB, Dong, X-M, Garg, M, Gery, S, Hattori, N, Huang, RY-J, Koeffler, HP, Lin, D-C, Liu, L-Z, Meng, X, Said, JW, Sun, Q-Y, Tang, K, Xiao, J-F, Yang, H   +16 more
core   +2 more sources

Evidence for In Vivo Phosphorylation of the Grb2 SH2-Domain Binding Site on Focal Adhesion Kinase by Src-Family Protein-Tyrosine Kinases [PDF]

Molecular and Cellular Biology, 1996
Focal adhesion kinase (FAK) is a nonreceptor protein-tyrosine kinase (PTK) that associates with integrin receptors and participates in extracellular matrix-mediated signal transduction events. We showed previously that the c-Src nonreceptor PTK and the Grb2 SH2/SH3 adaptor protein bound directly to FAK after fibronectin stimulation (D. D. Schlaepfer, S.
D D, Schlaepfer, T, Hunter
openaire   +2 more sources

SHP-2 Mediates Cryptosporidium parvum Infectivity in Human Intestinal Epithelial Cells. [PDF]

PLoS ONE, 2015
The parasite, Cryptosporidium parvum, induces human gastroenteritis through infection of host epithelial cells in the small intestine. During the initial stage of infection, C.
Eunice A Varughese, Susan Kasper, Emily M Anneken, Jagjit S Yadav   +3 more
doaj   +1 more source