In S. cerevisiae, SEY1 plays a crucial role in ER dynamics by mediating homotypic ER fusion, a process essential for maintaining ER morphology and function . SEY1 acts similarly to atlastins (ATLs) in other organisms, undergoing GTP-dependent dimerization to facilitate membrane tethering and fusion . The absence of SEY1 leads to abnormal ER morphology, characterized by reduced tubules and increased sheets .
Given the lack of information on a recombinant SEY1 protein from Candida albicans, future research could focus on:
Cloning and Expression: Investigating whether SEY1 can be cloned and expressed in Candida albicans, and if it retains similar functions as in S. cerevisiae.
Functional Analysis: Studying the potential roles of SEY1 in Candida albicans, if it exists or is engineered to exist, focusing on ER dynamics and cellular processes.
Comparative Studies: Comparing the functions of SEY1 across different organisms to understand its evolutionary conservation and potential applications.
| Protein | Organism | Function | Relevance to Candida albicans |
|---|---|---|---|
| SEY1 | S. cerevisiae | ER fusion | Potential for study in C. albicans |
| Dse1 | C. albicans | Cell wall integrity | Essential for virulence |
| Prn1 | C. albicans | Oxidative stress response | Important for survival under stress |
Hu et al. (2012): Dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae .
Dse1 in Candida albicans: Essential for cell wall integrity and virulence .
Plasmodium SEY1: A novel druggable target involved in ER membrane fusion .
Prn1 in Candida albicans: Involved in oxidative stress responses .
SEY1, a protein from Candida albicans, functions in the organization of the endoplasmic reticulum (ER) network. It interacts with reticulon proteins and DP1 family proteins to maintain the tubular ER structure. Its GTPase activity is essential for this ER organizational role.