AI Article Synopsis
- VPS45 is crucial for SNARE-mediated membrane fusion in endosomal trafficking, but its specific function is still unclear.
- A genetic suppressor screen revealed that a mutation in another SM protein, VPS33A, can counteract the negative effects of losing VPS45, specifically a temperature-sensitive lethality.
- The mutation (M376I) in VPS33A targets domain 3a, which is important for assembling SNARE complexes, emphasizing its significance in the function of endosomal SM proteins and membrane fusion processes.
Article Abstract
The Sec1/Munc18 (SM) protein VPS45 is a key regulator of SNARE-mediated membrane fusion in endosomal trafficking, but its precise role remains unknown. To understand the function of VPS45 , we performed a genetic suppressor screen in . We found that the temperature-sensitive lethality caused by the loss of VPS-45 can be suppressed by a mutation in another SM protein, VPS33A. The VPS33A M376I mutation is located in domain 3a, which is predicted to be essential for SNARE complex assembly. These results highlight the functional importance of domain 3a in endosomal SM proteins and its role in specific membrane fusion.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10995724 | PMC |
| http://dx.doi.org/10.17912/micropub.biology.001155 | DOI Listing |
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