And some keratin bands.

Hope it gets back online! Such a great tool.

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.

Thanks to Josh and all the students and post-docs for a great visit. Such a wonderful community doing great science!

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.

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.

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".

...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.

Third surprise: SURF4 can bind some clients co-translationally. This is not how we thought export receptors should work - we assumed that they would only bind fully folded cargoes, once they were competent for export. But the ER export signal is revealed after signal peptide cleavage, which is ...