Felix Randow
@felixrandow.bsky.social
Immunologist x cell biologist x microbiologist at MRC LMB in Cambridge. Occasionally birdwatching. Less nerdy than my bio sounds. Views my own.
Don't miss similar findings from the Coers and Pan labs in BiorXiv and NatComm. Also note that Burkholderia antagonizes LPS ubiquitylation through DUB action (Thurston lab) and that Chlamydia deploys GarD (Coers lab). Conclusion: Bacteria decided RNF213 is a hot target in host–pathogen warfare!
April 9, 2025 at 9:44 PM
Don't miss similar findings from the Coers and Pan labs in BiorXiv and NatComm. Also note that Burkholderia antagonizes LPS ubiquitylation through DUB action (Thurston lab) and that Chlamydia deploys GarD (Coers lab). Conclusion: Bacteria decided RNF213 is a hot target in host–pathogen warfare!
Remarkably, IpaH1.4 doesn’t stop at RNF213—it targets several host E3 ligases via their RING domains. Individual RINGs bind overlapping sites on IpaH1.4 through unique interactions, explaining specificity of IpaH1.4 towards select RING domains. A clever strategy!
April 9, 2025 at 9:44 PM
Remarkably, IpaH1.4 doesn’t stop at RNF213—it targets several host E3 ligases via their RING domains. Individual RINGs bind overlapping sites on IpaH1.4 through unique interactions, explaining specificity of IpaH1.4 towards select RING domains. A clever strategy!
Cryo-EM reveals IpaH1.4 binds the RING domain of RNF213—a region with no known E3 activity in RNF213. However, despite pressure from IpaH1.4, the RING is highly conserved, hinting at a key function. Intriguingly, Moyamoya disease–linked mutations also occur in this domain.
April 9, 2025 at 9:44 PM
Cryo-EM reveals IpaH1.4 binds the RING domain of RNF213—a region with no known E3 activity in RNF213. However, despite pressure from IpaH1.4, the RING is highly conserved, hinting at a key function. Intriguingly, Moyamoya disease–linked mutations also occur in this domain.
Who’ll get the second popcorn??
January 17, 2025 at 1:08 PM
Who’ll get the second popcorn??