All cellular proteins are made as long strings of amino acids called polypeptide chains. How these chains get folded into their unique 3‐dimensional shapes so they can perform their unique cellular functions remains an outstanding question in biology. It is known that cells use proteins called molecular chaperones to assist protein folding.
Our lab focuses on understanding the folding, assembly and trafficking of ciliary dynein motors that power the beating motion of eukaryotic cilia and flagella. A newly discovered family of proteins called Dynein Axonemal Assembly Factors (DNAAFs) cooperates with molecular chaperones to shepherd dynein assembly.
A key focus of this project is to dissect how chaperones and DNAAFs interact. Understanding their interactions is central to human biology as mis-folding/mis-assembly of ciliary dynein’s is a leading cause of infertility and a severe respiratory illness in humans called Primary Ciliary Dyskinesia (PCD).
We use a diverse set of techniques in the lab including cell culture, bioimaging, proteomics, biochemistry and structural studies. This project will combine several of these techniques to elucidate the molecular mechanisms of chaperones and DNAAFs in folding and assembling dynein motors.
Mali lab
Investigating how cells assemble axonemal dyneins, in particular the role of DNAAFs in this process
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