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Carboxyl‐Terminus of TFG Regulates Directional Movement of COPII Transport Carriers
Author(s) -
Block Samuel,
Hanna Michael,
Audhya Anjon
Publication year - 2017
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.31.1_supplement.760.12
Subject(s) - copii , endoplasmic reticulum , vesicle , microbiology and biotechnology , copi , cytosol , transport protein , secretory pathway , vesicular transport proteins , biology , secretory protein , biochemistry , chemistry , n terminus , membrane , golgi apparatus , secretion , peptide sequence , gene , enzyme
Roughly one fourth of all proteins encoded by the human genome are integral membrane proteins that participate in a large number of vital biochemical processes, such as ion transport and signal propagation. To achieve functionality, these proteins must travel through the secretory pathway, in which they are modified and trafficked to their specific organelles. The journey along the secretory pathway originates at subdomains on endoplasmic reticulum (ER) tubules, known as ER exit sites (ERES). Here, newly synthesized proteins embedded in the ER membrane, as well as soluble cargoes, are packaged into vesicles that bud off the ER in a process dependent on the COPII machinery. While the minimum components needed to generate a COPII vesicle have been identified, the mechanism that facilitates the coordinated anterograde transport of these carriers remains poorly understood. Our lab has previously identified TFG (Trk‐fused gene) as an essential component of the coordinated efflux of COPII vesicles from ERES. TFG contains an intrinsically disordered region at its carboxyl‐terminus capable of homo‐oligomerization in Vitro , and is essential for its co‐localization with COPII components in Vivo . Given these data, we hypothesized that the carboxyl‐terminus of TFG regulates the movement of COPII vesicles in a process dependent upon self‐oligomerization, as well as interactions with other components of COPII vesicles. To test this hypothesis, we used affinity chromatography with recombinant GST tagged TFG and a preparation of rat liver cytosol to isolate potential interacting partners, which can be further characterized by mass spectrometry.