Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions
Michael Warchol, Charles W Kroft, Jeffrey B Krall, Shaun Bevers, Robb Welty, Morkos A Henen, Beat Vögeli · 2026
Read Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions by Michael Warchol, Charles W Kroft, Jeffrey B Krall, Shaun Bevers, Robb Welty, Morkos A Henen, Beat Vögeli (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13635249.txt.
Description
Michael Warchol and six colleagues studied how chemical tags re-tune the cell's cargo-hauling motor. The motor, cytoplasmic dynein, drags loads along cell tracks via adaptor proteins gripping one of its chains. The team asked whether phosphate tags, added by a cell-division enzyme, change which adaptors grip and how tightly. They tagged the chain's tail in the lab and read the effects with magnetic resonance methods revealing protein shape and contacts.
Tagging did not rebuild the tail's loose structure, yet it rearranged the tail's long-range contacts. One adaptor, BICD2, touched the tail differently afterward, with little change in grip strength. The tags also opened a high-affinity docking site for the shape-editing protein Pin1. Once Pin1 sat down, it selectively loosened BICD2's grip while leaving two other adaptors alone. The authors describe a tag-and-editor switch fine-tuning cargo loading during busy cell periods.
Catalog record
| CREATOR | Michael Warchol, Charles W Kroft, Jeffrey B Krall, Shaun Bevers, Robb Welty, Morkos A Henen, Beat Vögeli |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 62 KB |
| LICENSE | http://creativecommons.org/licenses/by/4.0/). |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |