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Identifying Colocalization of the Rho GTPase TCL/RhoJ with Coronin Proteins at Vesicular Membranes
Author(s) -
McRoss Jasmine,
Anliker Clair,
Grigoryants Angelina,
Samuelson Chelsea,
Tader Brooke R,
Hamann Michael J
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.477.6
Subject(s) - gtpase , microbiology and biotechnology , guanine nucleotide exchange factor , rab , biology , cdc42 , vesicular transport protein , membrane , biochemistry , vesicle
The Rho‐family GTPase TCL/RhoJ has been shown to enhance pro‐angiogenic and pro‐metastatic cellular processes; however, less is known about the signaling pathways and protein binding partners regulating its activity. TCL is part of the Cdc42 subfamily of Rho GTPases and bears a short, unique N terminus that is important for GTP‐loading and localization to the plasma membrane. Additionally, we have evidence that TCL is held to vesicular membranes through a protein/protein interaction when it is specifically in the GDP‐loaded confirmation. As several coronin family proteins bind other Rho family GTPases when they are in a GDP‐loaded conformation, we are evaluating whether coronins also selectively and spatially interact with GDP‐loaded TCL. To determine if the coronins co‐localize with TCL at vesicular membranes, mCherry‐fused versions of several Homo sapiens coronin proteins will be transfected into HeLa cells along with YFP‐tagged versions of TCL bearing constitutively active and dominant negative mutations. These TCL mutations will mimic GTP and GDP bound forms of TCL and help identify nucleotide dependent interactions with coronin proteins. Given the importance of TCL in tumor‐associated angiogenesis, these results will provide valuable insights into additional binding partners of TCL and may help clarify its role in pro‐angiogenic processes. Support or Funding Information This work was supported by Bemidji State University Biology Department and the College of Business, Mathematics, and Science. Support was also provided through the Neilson Foundation, Bemidji, MN and Regenerative Medicine Minnesota (RMM‐2017‐EP‐04). This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .