Our paper explaining why two motor proteins that walk in opposite direction depend on each other is finally out. Great collaboration with @Carter_Lab, initiated by @zwetza, beautiful structural biology by @fe_aali. A thread 🧵 (1/9)

After 12 years, it's time to move on and go to where the sky is blue and the grass is greener. See you at annestraube@bsky.social #MyXAnniversary

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Our paper on the co-dependence of dynein and KIF1C is finally published in print: Congrats again to all involved: first authors @fe_aali and @zwetza who did most of the work and contributors from the @Carter_Lab Reposting explainer thread.

RT @Official_BSCB: One week left to submit an abstract for the @Co_Biologists 100 meeting incorporating the @Official_BSCB & @_BSDB_ an….

RT @christlet: Do you want to hear the latest and greatest about the neuronal cytoskeleton? Join us in Chile next April for #NeuroCyto2025,….

Leaving you with this beautiful summary drawn by @fe_aali

The KIF1C cargo binding region is sufficient to destabilise this conformation, open the adapter and allow dynein to bind. Thereby KIF1C helps both dynein to load onto cargo and extends its runs, explaining why these opposite polarity motors depend on each other. (8/9)

Using CryoEM, Alphafold2 and Crosslinking mass spectrometry, Ferdos could piece together the structure of the HOOK3 cargo adapter complex (FHF) and show that it is folded into a configuration that is not compatible with binding KIF1C or dynein. (7/9)

But the most dramatic effect was the activation of dynein by KIF1C (or just the bit of KIF1C that binds HOOK3), resulting in more dynein landing and running along microtubules. Likewise, dynein or just any part of the dynein machinery increased the activation of KIF1C. (6/9)

Alex observed motility in both directions, suggesting that motors are not in a tug-of-war. By dropping out components and removing the motor domains, he discovered that presence of the KIF1C motor resulted in longer dynein runs, i.e. was helping dynein to stay on track (5/9)

To understand motor co-dependence, we rebuilt the complex of KIF1C (plus directed motor) and dynein/dynactin (minus directed motor) linked by HOOK3 (the natural adapter that couples these motors to cargo) from purified, labelled proteins (4/9)

But we and others have observed that removing or disabling one of the motors in cells, results in reduced transport in both directions (see , a phenomenon called motor co-dependence. (3/9)

Usually if two opposite polarity motors are coupled together they undertake a tug-of-war. If the forces are balanced, transport would stall. If one set of motors is stronger, movement occurs, against the resistance of the other. (2/9) Image courtesy of OpenAIs DALL-E platform.

RT @DGZ_info: Join us on Monday noon for the #DGZ Focus Workshop on #Cytoskeleton & #MolecularMotors! Organized by @AnneStraube and Franzis….

RT @focalplane_jcs: Are you looking for your next job in #cellbio research? Check out our new cell biology jobs board on FocalPlane! So far….

Love making proteins and using microscopes? Interested in figuring out how molecular motors transport cargoes and organise microtubules? Join us as a postdoc. Apply here:

RT @Co_Biologists: We are excited to announce that registration is now open for Biologists @ 100, a unique conference to celebrate our 100….

Finished your Biochemistry degree, really like research, but no plans yet? Come and join us as a research assistant. We are looking for someone with experience in protein purification who wants to support our research projects on molecular motors. Apply:

Motors are out of Quarantine. Submit an abstract before 6th August for a talk in subgroup "Regulation of Molecular Motor Activity" at #cellbio2024.We will also host webinars in autumn, so if you want to talk in #MotorsInQuarantine, sign up here:

Keynote at #EESMicrotubules by the legendary Nobutaka Hirokawa - discoverer of so many kinesin superfamily proteins, their structural diversity and functions, explaining their involvement in various diseases.