Alexandra C. Newton
University of California, San Diego
238 Papers
3.6K Citations
Alexandra C. Newton is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Protein kinase C & Phosphorylation. The author has an hindex of 73, co-authored 218 publications. Previous affiliations of Alexandra C. Newton include Stanford University & University of California.
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Papers
INTERACTION OF PROTEINS WITH LIPID HEADGROUPS: Lessons from Protein Kinase C
TL;DR: The model for Protein Kinase C:Lipid Interaction is described as follows: Lipid-Induced Conformational Changes, followed by Lessons from PROTEIN KINASE C.
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Regulation of novel protein kinase C ε by phosphorylation
Vittoria Cenni,Heike Döppler,Erica Dutil Sonnenburg,Nadir M. Maraldi,Alexandra C. Newton,Alex Toker,Alex Toker +6 more
TL;DR: Analysis of the contribution of the phosphoinositide-dependent kinase 1 (PDK-1) and PKCepsilon kinase activity in controlling the phosphorylation of Thr(566) and Ser(729) reveals that the mechanism of phosphorylate of a novel PKC is the same as that for conventional PKCs: PDK- 1 phosphorylated of the activation loop triggers autophosphorylationof the hydrophobic motif.
Lipid activation of protein kinases.
TL;DR: This review addresses the molecular mechanisms by which PKC and Akt transduce signals propagated by the two major lipid second messenger pathways in cells, those of diacylglycerol signaling and phosphatidylinositol-3,4,5-trisphosphate (PIP3) signaling, respectively.
167
A Single Residue in the C1 Domain Sensitizes Novel Protein Kinase C Isoforms to Cellular Diacylglycerol Production
TL;DR: The finding that a single residue controls the affinity of the C1 domain for DAG-containing membranes provides a molecular explanation for why 1) DAG alone is sufficient to activate n PKCs but not cPKCs and 2) nPKCs target to the Golgi.
166
The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain.
TL;DR: This study establishes that each module is an independent membrane-targeting module with each, independently of the other, containing determinants for membrane recognition.
164