Recombinant Human Dynein light chain protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Dynein light chain also known as DLC is a component of the dynein protein complex. This complex functions as a motor protein driving cellular transport by walking along microtubules using ATP hydrolysis. Dynein light chain is small approximately 8 kDa in mass yet it plays an integral role in dynein’s mechanical operation. These proteins are ubiquitously expressed throughout various tissues in eukaryotic organisms including humans where they assist in the intracellular transport of organelles proteins and RNA.

Biological function summary

Dynein light chain is essential for the function and stability of the dynein motor complex which also includes heavy chains intermediate chains and other light chains. The dynein complex mediates the retrograde transport along axons and is involved in cell division by contributing to spindle positioning. Dynein light chain binds to cargo adaptor proteins and helps the dynein complex anchor to various cellular structures ensuring targeted transport within the cell.

Pathways

The dynein light chain plays an important role in the intracellular transport pathway particularly in vesicle trafficking and organelle positioning. It interacts with key proteins such as dynactin an important cofactor that enhances dynein's motor function and cargo binding. Additionally dynein light chain participates in mitotic spindle orientation collaborating with proteins like LIS1 to ensure proper chromosome segregation during mitosis.

Dysregulation of dynein light chain function is linked to neurodegenerative conditions such as Huntington's disease and motor neuron disorders. Alterations in dynein-mediated transport can lead to the accumulation of protein aggregates and impaired neural function. In Huntington’s disease this disruption affects the dynein and dynactin interaction contributing to neuronal dysfunction and cell death. Dynein light chain’s efficiency and integrity also intersect with LIS1 in lissencephaly where reduced dynein activity can result in abnormal neuronal migration and brain structure abnormalities.