Liz Miller
lizmillercu.bsky.social
Liz Miller
@lizmillercu.bsky.social
Cell Biologist at the University of Dundee, formerly at the MRC-LMB in Cambridge (UK) and Columbia University in NYC (USA). Interested in membrane traffic, protein quality control. Opinions my own. She/her.
And some keratin bands.
November 26, 2025 at 12:05 PM
Hope it gets back online! Such a great tool.
October 3, 2025 at 11:28 AM
Lovely work! Yeast polytopic proteins have fewer ribosomes than soluble proteins doi.org/10.1016/j.cu... likely reducing ribosome collisions. I wonder if you separate polytopics from single-pass MPs you see differences in codon use. We wondered about initiation but maybe codon use is also important.
Redirecting
doi.org
August 7, 2025 at 9:27 AM
Thanks to Josh and all the students and post-docs for a great visit. Such a wonderful community doing great science!
July 2, 2025 at 10:15 AM
I think it's a clamp. Provides structural rigidity but via protein-protein interfaces so it might be dynamic/malleable. Four complexes (so far - not privilege to Alex's info): Sec31 (the OG and only essential function in yeast), Sec16 (function unknown), NPC, GATOR.
May 18, 2025 at 1:51 PM
One last shout-out to @jcellbiol.bsky.social who handled an efficient, constructive and very fair peer review process. I know I'm biased because I'm an academic editor there, but this is now my go-to journal for our very best work.
November 13, 2024 at 8:14 AM
Finally, bioinformatic analysis by @xlichem.bsky.social systematically examined SURF4 export signals across the secretome, finding that cytokines/chemokines and proteases are most likely to access the "fast-track".
November 13, 2024 at 8:14 AM
...usually co-translational. Stalled translation products STILL bound SURF4 when folding could not have happened. We think this is a fast-track out of the ER for certain classes of proteins that have strong SURF4-binding motifs immediately downstream of their signal peptides.
November 13, 2024 at 8:14 AM