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18 results on '"Pearce, Sarah E."'

9. Performance and calibration of the AXAF High-Resolution Camera I: imaging readout

Author

Kenter, Almus T., primary, Chappell, John H., additional, Kobayashi, K., additional, Kraft, Ralph P., additional, Meehan, G. R., additional, Murray, Stephen S., additional, Zombeck, Martin V., additional, Fraser, George W., additional, Pearson, James F., additional, Lees, John E., additional, Brunton, Adam N., additional, Pearce, Sarah E., additional, Barbera, Marco, additional, Collura, Alfonso, additional, and Serio, Salvatore, additional

Published
1997
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10. AXAF High-Resolution Camera (HRC): calibration and recalibration at XRCF and beyond

Author

Murray, Stephen S., primary, Chappell, John H., additional, Kenter, Almus T., additional, Kobayashi, K., additional, Kraft, Ralph P., additional, Meehan, G. R., additional, Zombeck, Martin V., additional, Fraser, George W., additional, Pearson, James F., additional, Lees, John E., additional, Brunton, Adam N., additional, Pearce, Sarah E., additional, Barbera, Marco, additional, Collura, Alfonso, additional, and Serio, Salvatore, additional

Published
1997
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11. Absolute quantum efficiency calibration of the AXAF High-Resolution Camera

Author

Kraft, Ralph P., primary, Chappell, John H., additional, Kenter, Almus T., additional, Kobayashi, K., additional, Meehan, G. R., additional, Murray, Stephen S., additional, Zombeck, Martin V., additional, Fraser, George W., additional, Pearson, James F., additional, Lees, John E., additional, Brunton, Adam N., additional, and Pearce, Sarah E., additional

Published
1996
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13. Protein kinase D-mediated phosphorylation at Ser99 regulates localization of p21-activated kinase 4.

Author

BASTEA, Ligia I., DÖPPLER, Heike, PEARCE, Sarah E., DURAND, Nisha, SPRATLEY, Samantha J., and STORZ, Peter

Subjects
PROTEIN kinases, PHOSPHORYLATION, CELL migration, CELL motility, METASTASIS, PREVENTION
Abstract

PAKs (p21-activated kinases) are effectors of RhoGTPases. PAK4 contributes to regulation of cofilin at the leading edge of migrating cells through activation of LIMK (Lin-11/Isl-1/Mec-3 kinase). PAK4 activity is regulated by an autoinhibitory domain that is released upon RhoGTPase binding as well as phosphorylation at Ser474 in the activation loop of the kinase domain. In the present study, we add another level of complexity to PAK4 regulation by showing that phosphorylation at Ser99 is required for its targeting to the leading edge. This phosphorylation is mediated by PKD1 (protein kinase D1). Phosphorylation of PAK4 at Ser99 also mediates binding to 14-3-3 protein, and is required for the formation of a PAK4-LIMK-PKD1 complex that regulates cofilin activity and directed cell migration. [ABSTRACT FROM AUTHOR]

Published
2013
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