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Related Experiment Video

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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation

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Structural dynamics and multiregion interactions in dynein-dynactin recognition.

Jessica L Morgan¹, Yujuan Song, Elisar Barbar

¹Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331, USA.

The Journal of Biological Chemistry

|September 21, 2011

Summary

Cytoplasmic dynein and dynactin motor proteins interact via two key regions on the intermediate chain (IC). This interaction is crucial for cellular transport, with structural changes in IC regulating dynein-dynactin binding.

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Area of Science:

Molecular Biology
Cellular Dynamics
Protein Structure and Function

Background:

Cytoplasmic dynein is a major motor protein complex driving minus-end microtubule motility.
Dynactin acts as an activator, targeting dynein to cellular locations and linking it to cargo.
The p150(Glued) subunit of dynactin directly interacts with the dynein intermediate chain (IC) subunit.

Purpose of the Study:

To elucidate the structural basis of the interaction between dynactin's p150(Glued) subunit and the dynein intermediate chain (IC).
To characterize the binding footprint and affinity of p150(Glued) on IC.
To investigate the role of different regions within IC in dynein-dynactin complex formation and regulation.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy to determine protein structures and dynamics.
Isothermal Titration Calorimetry (ITC) to quantify binding affinities.
Analysis of spectral exchange broadening to infer structural changes upon binding.

Main Results:

The binding interface of p150(Glued) on IC consists of two distinct, noncontiguous recognition regions, both essential for high binding affinity.
In the absence of p150(Glued), IC exhibits helical structure in region 1, a nascent helix in region 2, and disorder elsewhere.
Upon p150(Glued) binding, region 1 forms a coiled-coil and region 2 a stable helix, while intervening segments remain disordered.
In the full 150-kDa complex, non-interface segments of the proteins remain disordered.

Conclusions:

The IC-p150(Glued) interaction involves a multi-region interface with dynamic structural elements.
The disorder in certain IC regions, potential for post-translational modification, and alternative splicing offer mechanisms for regulating dynein-dynactin binding.
The disordered linker region may serve as a platform for cargo recognition by dynein.