Addy Alt
Bar-Ilan University
22 Papers
553 Citations
Addy Alt is an academic researcher from Bar-Ilan University. The author has contributed to research in topics: Protein kinase C & Insulin. The author has an hindex of 11, co-authored 22 publications.
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Papers
Insulin Stimulates PKCζ-mediated Phosphorylation of Insulin Receptor Substrate-1 (IRS-1) A SELF-ATTENUATED MECHANISM TO NEGATIVELY REGULATE THE FUNCTION OF IRS PROTEINS
Yan-Fang Liu,Keren Paz,Avia Herschkovitz,Addy Alt,Tamar Tennenbaum,Sanford R. Sampson,Motoi Ohba,Toshio Kuroki,Derek LeRoith,Yehiel Zick +9 more
TL;DR: Findings implicate PKCzeta as a key element in a multistep negative feedback control mechanism of IRS-1 functions, in which insulin triggers a sequential cascade in which PI3K-mediated activation of PKCczeta inhibits IRS- 1 functions, reduces complex formation between IRS-2 andPI3K, and inhibits further activation ofPKCZeta itself.
193
Activation of Protein Kinase Cζ Induces Serine Phosphorylation of VAMP2 in the GLUT4 Compartment and Increases Glucose Transport in Skeletal Muscle
Liora Braiman,Addy Alt,Toshio Kuroki,Motoi Ohba,Asia Bak,Tamar Tennenbaum,Sanford R. Sampson +6 more
TL;DR: It is demonstrated that PKCζ regulates insulin-stimulated GLUT4 translocation and glucose transport through the unique colocalization of this isoform with theGLUT4 compartments.
104
Protein kinase Cdelta mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle.
Liora Braiman,Addy Alt,Toshio Kuroki,Motoi Ohba,Asia Bak,Tamar Tennenbaum,Sanford R. Sampson +6 more
TL;DR: It is found that insulin induces tyrosine phosphorylation and translocation of PKCcdelta to the plasma membrane and increases the activity of this isoform, and that activated PKCdelta is a major signaling molecule in insulin-induced glucose transport.
100
The role of protein kinase C delta activation and STAT3 Ser727 phosphorylation in insulin-induced keratinocyte proliferation.
TL;DR: PKCδ activation is a primary regulator of STAT3 serine phosphorylation and that PKCδ is essential in directing insulin-induced signaling in keratinocyte proliferation is indicated.