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CCSer2 gates dynein activity at the cell periphery.
Juliana L Zang1, Daytan Gibson1, Ann-Marie Zheng1
1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
Biorxiv : the Preprint Server for Biology
|June 25, 2024
Summary
CCSer2 is the first protein found to control cytoplasmic dynein-1 (dynein) motor activity spatially. It enables cell migration by regulating dynein at the cell periphery, activating it for specific cargo transport.
Area of Science:
- Cell Biology
- Molecular Motors
- Cell Migration
Background:
- Cytoplasmic dynein-1 (dynein) is a crucial microtubule motor protein responsible for intracellular transport of numerous cargos.
- Regulation of dynein's spatiotemporal activity is essential for cellular functions but remains poorly understood.
Purpose of the Study:
- To identify proteins that regulate dynein activity in specific cellular locations.
- To elucidate the mechanism by which dynein's spatial activity is controlled.
Main Methods:
- Identification of CCSer2 as a novel dynein-interacting protein.
- Investigating the role of CCSer2 in cell migration using zebrafish and human cell culture models.
- Analyzing the interaction between dynein, CCSer2, and its regulator Ndel1 at the cellular periphery.
Main Results:
- CCSer2 acts as a spatial gatekeeper for dynein activity, promoting cell migration.
- CCSer2 specifically inhibits the dynein-Ndel1 interaction at the cell periphery.
- This localized inhibition results in the activation of dynein for cargo trafficking at the cell cortex.
Conclusions:
- CCSer2 is the first identified protein to regulate dynein activity in the spatial dimension.
- Spatial specificity of dynein is achieved through localized proteins that disinhibit its regulator, Ndel1.
- CCSer2 represents a class of proteins that activate dynein in specific cellular microenvironments via Ndel1 inhibition.
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