Xin Xiang
xianglab.bsky.social
Xin Xiang
@xianglab.bsky.social
dynein, dynactin, Lis1, kinesin-1, Aspergillus nidulans as a genetic system. Opinions are my own.
Without these possibly impossible mutants, it is hard to falsify that LLPS may play a role somewhere in the process just as more specific protein-protein interactions. Both could be necessary (neither is sufficient). I have never worked on LLPS. These discussions are very helpful! Thanks!
November 30, 2025 at 4:20 PM
I enjoyed reading the paper! The mutant data is convincing that LLPS can’t be the sole driver of protein localization in cells. It would be even better to obtain mutations that disrupt LLPS and show no effect on cellular localization, but this must be hard given the nature of the interactions.
November 30, 2025 at 3:45 PM
Thank you Ferdos!
April 29, 2025 at 10:38 PM
Thank you so much Prasanna!
April 11, 2025 at 8:08 AM
Wow! Congratulations!
March 20, 2025 at 8:17 PM
Just learned about this amazing work! doi.org/10.1016/j.cub.2024.12.041
Redirecting
doi.org
March 7, 2025 at 11:15 AM
Interesting! I guess they may still have it to get rid of lactic acid produced in muscle.
February 6, 2025 at 11:26 PM
This is such a sad news! I remember talking to him at meetings many years ago and learning about the Rab11-centrosome connection…
January 18, 2025 at 1:58 PM
fusions in Aspergillus nidulans from different labs: Sec63-mRFP or Sec63-GFP labeling ER (Peñalva); GFP-RabE(Rab11) labeling post-Golgi vesicles (Peñalva); An-Nup49-GFP (and more) for nuclear pores (Osmani); PexK-GFP for peroxisomes (Hynes; Reck-Peterson) etc.
January 4, 2025 at 2:32 PM