scholarly journals Src Kinase Activity Is Essential for Osteoclast Function

2004 ◽  
Vol 279 (17) ◽  
pp. 17660-17666 ◽  
Author(s):  
Tsuyoshi Miyazaki ◽  
Archana Sanjay ◽  
Lynn Neff ◽  
Sakae Tanaka ◽  
William C. Horne ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Src Kinase ◽  
Osteoclast Function

scholarly journals Regulation of cytochrome c oxidase activity by c-Src in osteoclasts

2003 ◽  
Vol 160 (5) ◽  
pp. 709-718 ◽  
Author(s):  
Tsuyoshi Miyazaki ◽  
Lynn Neff ◽  
Sakae Tanaka ◽  
William C. Horne ◽  
Roland Baron
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Kinase Activity ◽  
Src Kinase ◽  
Peptide Hormone ◽  
Inhibitory Effect ◽  
Normal Function ◽  
Nonreceptor Tyrosine Kinase ◽  
Extracellular Stimuli ◽  
Osteoclast Function

The function of the nonreceptor tyrosine kinase c-Src as a plasma membrane–associated molecular effector of a variety of extracellular stimuli is well known. Here, we show that c-Src is also present within mitochondria, where it phosphorylates cytochrome c oxidase (Cox). Deleting the c-src gene reduces Cox activity, and this inhibitory effect is restored by expressing exogenous c-Src. Furthermore, reducing endogenous Src kinase activity down-regulates Cox activity, whereas activating Src has the opposite effect. Src-induced Cox activity is required for normal function of cells that require high levels of ATP, such as mitochondria-rich osteoclasts. The peptide hormone calcitonin, which inhibits osteoclast function, also down-regulates Cox activity. Increasing Src kinase activity prevented the inhibitory effect of calcitonin on Cox activity and osteoclast function. These results suggest that c-Src plays a previously unrecognized role in maintaining cellular energy stores by activating Cox in mitochondria.

ADAM12 localizes with c-Src to actin-rich structures at the cell periphery and regulates Src kinase activity

2010 ◽  
Vol 316 (1) ◽  
pp. 55-67 ◽  
Author(s):  
Dorte Stautz ◽  
Archana Sanjay ◽  
Matilde Thye Hansen ◽  
Reidar Albrechtsen ◽  
Ulla M. Wewer ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Src Kinase ◽  
Cell Periphery

Src kinase activity is required for avoidance memory formation and recall

2003 ◽  
Vol 14 (8) ◽  
pp. 649-652 ◽  
Author(s):  
L. R. M. Bevilaqua ◽  
J. I. Rossato ◽  
J. H. Medina ◽  
I. Izquierdo ◽  
M. Cammarota
Keyword(s):  
Kinase Activity ◽  
Src Kinase ◽  
Memory Formation ◽  
Avoidance Memory

The spin trapping agent PBN stimulates H2O2-induced Erk and Src kinase activity in human neuroblastoma cells

Neuroreport ◽  
2002 ◽  
Vol 13 (8) ◽  
pp. 1057-1061 ◽  
Author(s):  
Pelin Kelicen ◽  
Ippolita Cantuti-Castelvetri ◽  
Can Pekiner ◽  
K. Eric Paulson
Keyword(s):  
Kinase Activity ◽  
Neuroblastoma Cells ◽  
Src Kinase ◽  
Spin Trapping ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Trapping Agent

Identification of potential biomarkers for measuring inhibition of Src kinase activity in colon cancer cells following treatment with dasatinib

2006 ◽  
Vol 5 (12) ◽  
pp. 3014-3022 ◽  
Author(s):  
Alan Serrels ◽  
Iain R.J. Macpherson ◽  
T.R. Jeffry Evans ◽  
Francis Y. Lee ◽  
Edwin A. Clark ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cancer Cells ◽  
Kinase Activity ◽  
Src Kinase ◽  
Colon Cancer Cells ◽  
Potential Biomarkers

Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis

1993 ◽  
Vol 13 (3) ◽  
pp. 1464-1470
Author(s):  
S Bagrodia ◽  
S J Taylor ◽  
D Shalloway
Keyword(s):  
Kinase Activity ◽  
Tyrosine Phosphatase ◽  
Src Kinase ◽  
Indirect Evidence ◽  
Membrane Localization ◽  
Wild Type ◽  
Src Tyrosine Kinase ◽  
Amino Terminal ◽  
Membrane Bound ◽  
Type C

The chicken proto-oncoprotein c-Src is phosphorylated by p34cdc2 during mitosis concomitant with increased c-Src tyrosine kinase activity. On the basis of indirect evidence, we previously suggested that this is caused by partial dephosphorylation at Tyr-527, the phosphorylation of which suppresses c-Src kinase activity. In support of this hypothesis, we now show that treatment of cells with a protein tyrosine phosphatase inhibitor, sodium vanadate, blocks the mitotic increase in Src kinase activity. Also, we show that an amino-terminal mutation that prevents myristylation (and membrane localization) of c-Src does not interfere with the p34cdc2-mediated phosphorylations but blocks both mitotic dephosphorylation of Tyr-527 (in kinase-defective Src) and stimulation of c-Src kinase activity. Furthermore, in unsynchronized cells, the kinase activity of nonmyristylated c-Src is suppressed by 60% relative to wild-type c-Src, presumably because of increased Tyr-527 phosphorylation. Consistent with this, the Tyr-527 dephosphorylation rate measured in cell homogenates is much higher for wild-type, myristylated c-Src than for nonmyristylated c-Src. Tyr-527 phosphatase activity was primarily associated with the nonsoluble subcellular fraction. These findings suggest that the phosphatase(s) that acts on Tyr-527 is membrane bound and indicate that membrane localization of c-Src is necessary for its mitotic activation by dephosphorylation of Tyr-527.

Activation of c-Src in cells bearing v-Crk and its suppression by Csk

1992 ◽  
Vol 12 (10) ◽  
pp. 4706-4713
Author(s):  
H Sabe ◽  
M Okada ◽  
H Nakagawa ◽  
H Hanafusa
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Src Kinase ◽  
Cellular Protein ◽  
Morphological Transformation ◽  
Protein Tyrosine ◽  
In Cells

The protein product of the CT10 virus, p47gag-crk (v-Crk), which contains Src homology region 2 (SH2) and 3 (SH3) domains but lacks a kinase domain, is believed to cause an increase in cellular protein tyrosine phosphorylation. A candidate tyrosine kinase, Csk (C-terminal Src kinase), has been implicated in c-Src Tyr-527 phosphorylation, which negatively regulates the protein tyrosine kinase of pp60c-src (c-Src). To investigate how c-Src kinase activity is regulated in vivo, we first looked at whether v-Crk can activate c-Src kinase. We found that cooverexpression of v-Crk and c-Src caused elevation of c-Src kinase activity, resulting in an increase of tyrosine phosphorylation of cellular proteins and morphological transformation of rat 3Y1 fibroblasts. v-Crk and c-Src complexes were not detected, although v-Crk bound to a variety of tyrosine-phosphorylated proteins in cells overexpressing v-Crk and c-Src. Overexpression of Csk in these transformed cells caused reversion to normal phenotypes and also reduced the level of c-Src kinase activity. However, Csk did not cause reversion of cells transformed by v-Src or c-Src527F, in which Tyr-527 was changed to Phe. These results strongly suggest that Csk acts on Tyr-527 of c-Src and suppresses c-Src kinase activity in vivo. Because Csk can suppress transformation by cooverexpression of v-Crk and c-Src, we suggest that v-Crk causes activation of c-Src in vivo by altering the phosphorylation state of Tyr-527.

Investigation of the effect of varying the 4-anilino and 7-alkoxy groups of 3-quinolinecarbonitriles on the inhibition of Src kinase activity

2003 ◽  
Vol 13 (21) ◽  
pp. 3797-3800 ◽  
Author(s):  
Diane H. Boschelli ◽  
Fei Ye ◽  
Biqi Wu ◽  
Yanong D. Wang ◽  
Ana Carolina Barrios Sosa ◽  
...  
Keyword(s):  
Kinase Activity ◽  
Src Kinase ◽  
Alkoxy Groups

scholarly journals Src Kinase Activity Is Required for Integrin αVβ3-Mediated Activation of Nuclear Factor-κB

2005 ◽  
Vol 280 (13) ◽  
pp. 12145-12151 ◽  
Author(s):  
Donald L. Courter ◽  
Lucy Lomas ◽  
Marta Scatena ◽  
Cecilia M. Giachelli
Keyword(s):  
Kinase Activity ◽  
Src Kinase ◽  
Integrin Αvβ3 ◽  
Nuclear Factor Κb ◽  
Nuclear Factor
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