The Cytospin-A (Cytokinesis And Spindle Organization A) protein is involved in several aspects of cell biology and is expressed in many tissues.  The Cytospin-A protein associates with both tubulin and actin filaments, and loss of Cytospin-A results in cytokinesis, cell adhesion, and gap junction defects.  The human Mono-Polar Spindles (hMps1) protein kinase is involved in the spindle assembly checkpoint and cytokinesis.  The Cytospin-A protein contains calponin homology (CH) and coiled coil (CC) domains, and a segment of the protein (amino acids 45-659) was previously isolated in a yeast 2-hybrid screen with the amino terminus (amino acids 1-311) of hMps1.  Amino acids 1-311 of hMps1 contain a tetratricopeptide repeat (TPR) and a crystal structure for the hMps1 TPR has been solved.  In silico modeling was used to predict Cytospin-A CC domain structure and dock the structure to the hMps1 TPR.  Modeling suggests the Cytospin-A CC domain forms paired alpha helical coils, and docking results indicate a groove within the hMps1 TPR interacts with specific residues within the Cytospin-A CC domain.  The cellular function of the interaction between Cytospin-A and hMps1 is not well characterized.  Cytospin-A functions to interact with and stabilize the cellular structural framework including the actin and microtubule networks.  The results of the in silico modeling presented here may enable improved understanding of the interaction between these two proteins and the role it plays in cell biology.

In silico modeling of cytospin-A coiled coil domain and docking with hMps1 tetratricopeptide repeat

ACS Spring Meeting 2021

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