Hugh F. Paterson

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Corrigendum to “Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active” [Cell Signal 23 (2011) 468–477]

Peter H. Sugden, Thomais Markou, Stephen J. Fuller, El Li Tham, more

Cellular Signalling > 2011 > 23 > 5 > 950

article

Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active

Peter H. Sugden, Thomais Markou, Stephen J. Fuller, El Li Tham, more

Cellular Signalling > 2011 > 23 > 2 > 468-477

ERK1 and ERK2 (ERK1/2) are central to the regulation of cell division, growth and survival. They are activated by phosphorylation of the Thr- and the Tyr- residues in their Thr-Glu-Tyr activation loops. The dogma is that dually-phosphorylated ERK1/2 constitute the principal activities in intact cells. We previously showed that, in neonatal rat cardiac myocytes, endothelin-1 and phorbol 12-myristate...

article

Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon

Tom D. Bunney, Richard Harris, Natalia Lamuño Gandarillas, Michelle B. Josephs, more

Molecular Cell > 2006 > 21 > 4 > 495-507

Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies of ras/effector interactions have focused on three classes, Raf kinases, ral guanylnucleotide-exchange factors, and phosphatidylinositol-3-kinases. Here we describe ras interactions with another effector, the recently identified phospholipase C epsilon (PLCɛ). We solved structures of PLCɛ RA domains...

article

RalGDS is required for tumor formation in a model of skin carcinogenesis

Ana González-García, Catrin A. Pritchard, Hugh F. Paterson, Georgia Mavria, more

Cancer Cell > 2005 > 7 > 3 > 219-226

To investigate the role of signaling by the small GTPase Ral, we have generated mice deficient for RalGDS, a guanine nucleotide exchange factor that activates Ral. We show that RalGDS is dispensable for mouse development but plays a substantial role in Ras-induced oncogenesis. Lack of RalGDS results in reduced tumor incidence, size, and progression to malignancy in multistage skin carcinogenesis,...

article

Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2

Rachel Ben-Levy, Steven Hooper, Rebecca Wilson, Hugh F. Paterson, more

Current Biology > 1998 > 8 > 19 > 1049-1057

Background: Mitogen-activated protein (MAP) kinases (or extracellular signal regulated kinases; Erks) and stress-activated protein (SAP) kinases mediate cellular responses to a wide variety of signals. In the Erk MAP kinase pathway, activation of MAP kinases takes place in the cytoplasm and the activated enzyme moves to the nucleus. This translocation to the nucleus is essential to MAP kinase signalling...

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Search results for: Hugh F. Paterson

Corrigendum to “Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active” [Cell Signal 23 (2011) 468–477]

Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active

Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon

RalGDS is required for tumor formation in a model of skin carcinogenesis

Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2

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INFONA - science communication portal

Search results for: Hugh F. Paterson

Corrigendum to “Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active” [Cell Signal 23 (2011) 468–477]

Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active

Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon

RalGDS is required for tumor formation in a model of skin carcinogenesis

Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2

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