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Regulation of Vesicle Formation at the Golgi Complex by the Arf GEFs Gea1 and Gea2
Author(s) -
Muccini Arnold,
Brownfield Bryce,
Gustafson Margaret,
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.657.2
Subject(s) - golgi apparatus , guanine nucleotide exchange factor , gtpase , microbiology and biotechnology , copi , adp ribosylation factor , small gtpase , biology , vesicle , chemistry , secretory pathway , biochemistry , signal transduction , endoplasmic reticulum , membrane
In eukaryotes, vesicle formation at the Golgi complex is initiated by the conserved small GTPase Arf1. In budding yeast, Arf1 localization and activity is controlled by three separate guanine nucleotide exchange factors (GEFs) Gea1, Gea2, and Sec7. Sec7 activates Arf1 at the trans ‐Golgi network, and mechanisms regulating the activity and recruitment of Sec7 to the Golgi have been well characterized. For example, Sec7 is recruited to the TGN by four small GTPases including its substrate Arf1. However, Gea1 and Gea2, which activate Arf1 at earlier Golgi compartments, do not share the same regulatory mechanisms as Sec7. While initially thought to be redundant paralogs, we have found that Gea1 and Gea2 localize to separate regions of the Golgi despite sharing common regulatory elements. As such, the purpose and mechanism for their differential localization remains unclear. I aim to understand the functional relevance for their distinct localization and will present preliminary evidence suggesting that Gea recruitment is coordinated by Golgi SNARE complexes. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .