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Jeffrey H. Stack

Researcher at University of California, San Diego

Publications -  16
Citations -  2454

Jeffrey H. Stack is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Vacuolar protein sorting & Vacuolar Sorting Protein VPS15. The author has an hindex of 11, co-authored 16 publications receiving 2405 citations. Previous affiliations of Jeffrey H. Stack include Howard Hughes Medical Institute & California Institute of Technology.

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Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting

TL;DR: Overexpression of VPS34p resulted in an increase in PI 3-kinase activity, and this activity was specifically precipitated with antisera to Vps34p.
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A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole.

TL;DR: It is proposed that Vps15p and Vps34p function together as components of a membrane‐associated signal transduction complex that regulates intracellular protein trafficking decisions through protein and lipid phosphorylation events.
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Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast.

TL;DR: Analysis of a temperature-conditional allele of VPS15 and of the defects in cellular PtdIns(3)P levels in various vps15 and vsp34 mutant strains has led to additional insights into the importance of Ptdins 3- kinase activity in intracellular localization, as well as the roles of Vps15p and Vps34p in vacuolar protein sorting.
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Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities.

TL;DR: It is proposed that the production of a specific phosphoinositide, PtdIns(3)P, is involved in regulating intracellular protein sorting reactions in eukaryotic cells.
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A novel protein kinase homolog essential for protein sorting to the yeast lysosome-like vacuole

TL;DR: The VPS15 gene encodes a novel protein kinase homolog that is essential for the efficient delivery of soluble hydrolases to the yeast vacuole and it is proposed that protein phosphorylation may act as a molecular "switch" within intracellular protein sorting pathways by actively diverting proteins from a default transit pathway to an alternative pathway.