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Full-Text Articles in Life Sciences
Yeast Dynamin And Ypt6 Converge On The Garp For Endosome-To-Golgi Trafficking, Pelin Makaraci
Yeast Dynamin And Ypt6 Converge On The Garp For Endosome-To-Golgi Trafficking, Pelin Makaraci
MSU Graduate Theses
Protein recycling is an important cellular process required for cell homeostasis. Results from prior studies demonstrated that Vps1, a dynamin homologue in yeast, is implicated in protein recycling from the endosome to the trans-Golgi Network (TGN). However, the function of Vps1 in relation to Ypt6, a master GTPase in the recycling pathway, remains unknown. The present study reveals that Vps1 physically interacts with Ypt6 if at least one of them is full-length. It was found that overexpression of full-length Vps1, but not GTP hydrolysis-defective Vps1 mutants, is sufficient to rescue abnormal phenotypes in membrane trafficking pathways provoked by loss …
Yeast Dynamin Associates With The Garp Tethering Complex For Endosome-To-Golgi Traffic, Uma Saimani
Yeast Dynamin Associates With The Garp Tethering Complex For Endosome-To-Golgi Traffic, Uma Saimani
MSU Graduate Theses
Yeast dynamin, Vacuolar Protein Sorting 1 (Vps1), has been implicated in recycling proteins and lipids from the endosome to the trans-Golgi network (TGN). Previous research showed a genetic interaction of Vps1 with all components of the GARP tethering complex, which anchors vesicles at the late Golgi membrane. I used the yeast two-hybrid system and pinpointed a 33 amino acid segment of Vps51, a GARP subunit, that interacts with Vps1. Based on sequence homology between Vps51 and its mammalian homolog ANG2 in the 33 amino acid stretch, I identified two key residues of Vps51, E127, and Y129, that bind Vps1. The …
Yeast Dynamin Functions With Escrt-Ii At The Late Endosome And Potential Roles With Novel Binding Partners, Bryan Thien Banh
Yeast Dynamin Functions With Escrt-Ii At The Late Endosome And Potential Roles With Novel Binding Partners, Bryan Thien Banh
MSU Graduate Theses
Yeast dynamin, Vps1, is a dynamic protein implicated in multiple trafficking pathways and at several cellular locations including the Golgi, endosome, and vacuole. Previous studies have found that Vps1 genetically and physically interacts with several ESCRT-II (Vps22, Vps36) and ESCRT-III (Vps2, Vps24) components. In light of these findings, little is known about how Vps1 functions with the ESCRT system. In my study, I have mapped the interaction domains between Vps1 and Vps22/Vps36 as well as explored the potential roles of these proteins during the targeting of vacuolar hydrolase, Cps1. My results support the idea of Vps1 working at the endosomal …
Functional Connection Between Yeast Dynamin And Retromer At The Endosome, Christopher Robert Trousdale
Functional Connection Between Yeast Dynamin And Retromer At The Endosome, Christopher Robert Trousdale
MSU Graduate Theses
Intracellular trafficking from the late endosome to Golgi in cells is termed retrograde transport, essential for recycling of important macromolecules including cell membrane receptors. Retrograde transport is regulated by a family of proteins known as the "Retromer” composed of 5 VPS proteins (Vps5, Vps17, Vps26, Vps29, and Vps35). Retromer acts as the coat proteins for vesicles emerging from late endosomes. Loss of Retromer function has been previously implicated in both Parkinson's and Alzheimer's disease. Vps1, a yeast dynamin-like protein, plays a role in intracellular trafficking. Vps1 has been shown to localize at the endocytic sites to promote pinching off of …
Dynamin Association With Clathrin And Its Physiological Roles At The Golgi And Targeting Mechanism To The Golgi, Shiva Kumar Goud Gadila
Dynamin Association With Clathrin And Its Physiological Roles At The Golgi And Targeting Mechanism To The Golgi, Shiva Kumar Goud Gadila
MSU Graduate Theses
Vps1 (Vacuole protein sorting 1), a dynamin-like protein in yeast, is implicated in diverse membrane trafficking pathways and localized to many organelles, including the Golgi. It has been proposed that Vps1 is functionally linked to clathrin heavy chain 1 (Chc1), but the question of how, where, and when they function together remains unknown. Lines of evidence suggest that Chc1 and Vps1 are located at the late Golgi. Therefore, I hypothesized that Vps1 binds to Chc1 and functions together at the Golgi for efficient Golgi-to-endosome membrane trafficking. Using the yeast-two hybrid assay, I present evidence that Vps1 binds to the C-terminal …