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Investigating regulation of the PI 4‐kinase Pik1 at the Saccharomyces cerevisiae trans ‐golgi network
Author(s) -
Diefenderfer Carolyn M,
Fromme J. Christopher
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.659.1
Subject(s) - saccharomyces cerevisiae , gtpase , golgi apparatus , microbiology and biotechnology , vesicle , small gtpase , vesicular transport protein , adp ribosylation factor , biology , chemistry , biochemistry , gene , signal transduction , membrane , endoplasmic reticulum
Vesicle‐mediated protein transport among eukaryotic cellular compartments is dynamic and tightly‐regulated. At the Saccharomyces cerevisiae t rans ‐ G olgi N etwork (TGN), the conserved small GTPases Ypt31 (Rab11 homologue) and Arf1 collaborate with an essential pool of phosphatidylinositol 4‐phosphate (PI4P) to recruit vesicle coats, vesicle transport motors, and tethering proteins to nascent outbound vesicles. The conserved lipid kinase Pik1 (PI4KIIIβ homologue) generates PI4P at the TGN, and work in several model systems suggests that it is regulated by close ties to the activities of Ypt31, Arf1, and the ArfGEF ( g uanine nucleotide e xchange f actor) Sec7 (BIG1/2 homologue). However, the mechanisms underlying this regulatory network are unclear. Using a combination of imaging and in vitro protein‐protein interaction studies, we have found that Pik1 relies on Sec7‐activated Arf1 for proper localization to the TGN and may, once at the TGN, influence the activity of Ypt31. Together, these data provide a clearer picture of how cooperation among Ypt31, Arf1, and Pik1/PI4P choreographs trafficking from the TGN. Support or Funding Information NSF GRFP DGE‐1650441; NIH/NIGMS This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .